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Conserved domains on  [gi|1339977384|gb|AUZ66810|]
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chemotaxis protein CheA [Citrobacter sp. CFNIH10]

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
 3-676 0e+00

chemotaxis protein CheA; Provisional


:

Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   3 MDISDFYQTFFDEADELLADMEQHLLDLAPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  83 LNTAIINLFLETKDIMQEQLDAYKSSQEPDAASFEYICTALRQLALEAKGETAPAVVANARLSVVDNTTPDDVVVAEEAK 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 163 LRIFLSRLKASEVALLEEELGNLSTLSDVVKGEDRLAATLDGDIAEDDVIAVLCFVIEADQIAFEKVVTATAPAVQPEVS 242
Cdd:PRK10547  161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEETTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 243 EVAEVvaveQPVVAVPAVKAVGREAQTGRVEREKPARASESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPVNH 322
Cdd:PRK10547  241 VVEVS----PKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNH 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 323 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 402
Cdd:PRK10547  317 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 403 SLDHGIELPEKRMESGKNVVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDDEVGMLIFAPGFS 482
Cdd:PRK10547  397 SLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFS 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 483 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPRDD 562
Cdd:PRK10547  477 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREE 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 563 DLHPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 642
Cdd:PRK10547  557 DLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 636

                         650       660       670
                  ....*....|....*....|....*....|....
gi 1339977384 643 SAATILGDGSVALIVDVSALQGLNREQRMAITAA 676
Cdd:PRK10547  637 SAATILGDGSVALIVDVSALQALNREQRMANTAA 670
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-676 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   3 MDISDFYQTFFDEADELLADMEQHLLDLAPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  83 LNTAIINLFLETKDIMQEQLDAYKSSQEPDAASFEYICTALRQLALEAKGETAPAVVANARLSVVDNTTPDDVVVAEEAK 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 163 LRIFLSRLKASEVALLEEELGNLSTLSDVVKGEDRLAATLDGDIAEDDVIAVLCFVIEADQIAFEKVVTATAPAVQPEVS 242
Cdd:PRK10547  161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEETTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 243 EVAEVvaveQPVVAVPAVKAVGREAQTGRVEREKPARASESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPVNH 322
Cdd:PRK10547  241 VVEVS----PKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNH 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 323 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 402
Cdd:PRK10547  317 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 403 SLDHGIELPEKRMESGKNVVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDDEVGMLIFAPGFS 482
Cdd:PRK10547  397 SLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFS 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 483 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPRDD 562
Cdd:PRK10547  477 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREE 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 563 DLHPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 642
Cdd:PRK10547  557 DLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 636

                         650       660       670
                  ....*....|....*....|....*....|....
gi 1339977384 643 SAATILGDGSVALIVDVSALQGLNREQRMAITAA 676
Cdd:PRK10547  637 SAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-675 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 706.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   3 MDISDFYQTFFDEADELLADMEQHLLDLAPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQ 82
Cdd:COG0643     1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  83 LNTAIINLFLETKDIMQEQLDAYKSSQEPDAASFEyictalrqlaleakgetapavvanarlsvvdnttpddvvvaeeak 162
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 163 lriFLSRLKASEVALLEEelgnlstlsdvvkgedrlaatldgdiaeddviavlcfVIEADQIAFEKVVTATAPAVQPevs 242
Cdd:COG0643   116 ---LLARLDASEEAIEEV-------------------------------------VADEVEISPPAPAALEPAPAAA--- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 243 evaevvaveqpvvavpavkavgreAQTGRVEREKPARASESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPVNH 322
Cdd:COG0643   153 ------------------------PPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESL 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 323 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 402
Cdd:COG0643   209 RELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRN 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 403 SLDHGIELPEKRMESGKNVVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDDEVGMLIFAP 479
Cdd:COG0643   289 AVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELLELIFAP 368

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 480 GFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQP 559
Cdd:COG0643   369 GFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRL 448

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 560 RDDDLHPLAGGErVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKV 639
Cdd:COG0643   449 DPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRV 527

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 1339977384 640 PGISAATILGDGSVALIVDVSALQGLNREQRMAITA 675
Cdd:COG0643   528 PGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 354-528 1.58e-93

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: 286.79  E-value: 1.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 354 VFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRMESGKNVVGNLILSAEHQG 433
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 434 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDDEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 510
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 1339977384 511 VEIQSKQGTGTTIRILLP 528
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
524-662 1.53e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 110.80  E-value: 1.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  524 RILLPLTLAILDgmsvrvaDEVFILPLNAVMESLQPRDDDL--HPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEAtQ 601
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339977384  602 GIVVILQSGGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 662
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 536-662 1.78e-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: 107.67  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 536 GMSVRVADEVFILPLNAVMESLQPRDDDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVEGAKTEaTQGIVVILQSGGRR 613
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339977384 614 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 662
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 3-676 0e+00

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 1388.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   3 MDISDFYQTFFDEADELLADMEQHLLDLAPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQ 82
Cdd:PRK10547    1 MDISDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  83 LNTAIINLFLETKDIMQEQLDAYKSSQEPDAASFEYICTALRQLALEAKGETAPAVVANARLSVVDNTTPDDVVVAEEAK 162
Cdd:PRK10547   81 LNTDIINLFLETKDIMQEQLDAYKTSQEPDAASFEYICQALRQLALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 163 LRIFLSRLKASEVALLEEELGNLSTLSDVVKGEDRLAATLDGDIAEDDVIAVLCFVIEADQIAFEKVVTATAPAVQPEVS 242
Cdd:PRK10547  161 LRIILSRLKAGEVDLLEEELGNLGTLTDVVKGADSLEATLPGSVAEDDITAVLCFVIEADQITFETAVAAPQEKAEETTE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 243 EVAEVvaveQPVVAVPAVKAVGREAQTGRVEREKPARASESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPVNH 322
Cdd:PRK10547  241 VVEVS----PKISVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSELDPVNH 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 323 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 402
Cdd:PRK10547  317 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 403 SLDHGIELPEKRMESGKNVVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGMAVNENMTDDEVGMLIFAPGFS 482
Cdd:PRK10547  397 SLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSENMSDEEVGMLIFAPGFS 476

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 483 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPRDD 562
Cdd:PRK10547  477 TAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREE 556

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 563 DLHPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 642
Cdd:PRK10547  557 DLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGI 636

                         650       660       670
                  ....*....|....*....|....*....|....
gi 1339977384 643 SAATILGDGSVALIVDVSALQGLNREQRMAITAA 676
Cdd:PRK10547  637 SAATILGDGSVALIVDVSALQALNREQRMANTAA 670
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
3-675 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 706.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   3 MDISDFYQTFFDEADELLADMEQHLLDLAPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQ 82
Cdd:COG0643     1 MDMDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  83 LNTAIINLFLETKDIMQEQLDAYKSSQEPDAASFEyictalrqlaleakgetapavvanarlsvvdnttpddvvvaeeak 162
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPADISA--------------------------------------------- 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 163 lriFLSRLKASEVALLEEelgnlstlsdvvkgedrlaatldgdiaeddviavlcfVIEADQIAFEKVVTATAPAVQPevs 242
Cdd:COG0643   116 ---LLARLDASEEAIEEV-------------------------------------VADEVEISPPAPAALEPAPAAA--- 152

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 243 evaevvaveqpvvavpavkavgreAQTGRVEREKPARASESTSIRVAVEKVDQLINLVGELVITQSMLAQRSNELDPVNH 322
Cdd:COG0643   153 ------------------------PPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESL 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 323 GDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 402
Cdd:COG0643   209 RELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRN 288

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 403 SLDHGIELPEKRMESGKNVVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAISQGM---AVNENMTDDEVGMLIFAP 479
Cdd:COG0643   289 AVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLitaEEAAALSDEELLELIFAP 368

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 480 GFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQP 559
Cdd:COG0643   369 GFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRL 448

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 560 RDDDLHPLAGGErVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSGGRRYALLVDQLIGQHQVVVKNLESNYRKV 639
Cdd:COG0643   449 DPDDIETVEGRE-VIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRV 527

                         650       660       670
                  ....*....|....*....|....*....|....*.
gi 1339977384 640 PGISAATILGDGSVALIVDVSALQGLNREQRMAITA 675
Cdd:COG0643   528 PGISGATILGDGRVALILDVAALVRSARARARAAAA 563
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 354-528 1.58e-93

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: 286.79  E-value: 1.58e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 354 VFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRMESGKNVVGNLILSAEHQG 433
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 434 GNICIEVTDDGAGLNRERILAKAISQGMAVNE---NMTDDEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGH 510
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADeaaTLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 1339977384 511 VEIQSKQGTGTTIRILLP 528
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 531-662 1.30e-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: 1.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 531 LAILDGMSVRVADEVFILPLNAVMESLQPRDDDLHPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSG 610
Cdd:cd00731     1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339977384 611 GRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 662
Cdd:cd00731    81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 533-662 2.97e-29

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: 112.75  E-value: 2.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 533 ILDGMSVRVADEVFILPLNAVMESLQPRDDDLHPLA--GGERVLEVRGEYLPLVELWKVFEVEGAKTEATQGIVVILQSG 610
Cdd:cd00588     1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPNApdYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1339977384 611 GRRYALLVDQLIGQHQVVVKNLESNY----RKVPGISAATILGDGSVALIVDVSAL 662
Cdd:cd00588    81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
CheW smart00260
Two component signalling adaptor domain;
524-662 1.53e-28

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 110.80  E-value: 1.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  524 RILLPLTLAILDgmsvrvaDEVFILPLNAVMESLQPRDDDL--HPLAGGERVLEVRGEYLPLVELWKVFEVEGAKTEAtQ 601
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRPPPITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPPEPPTD-E 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1339977384  602 GIVVILQSGGRRYALLVDQLIGQHQVVVKNLES----NYRKVPGISAATILGDGSVALIVDVSAL 662
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 536-662 1.78e-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: 107.67  E-value: 1.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 536 GMSVRVADEVFILPLNAVMESLQPRDDDLHPLAGG--ERVLEVRGEYLPLVELWKVFEVEGAKTEaTQGIVVILQSGGRR 613
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPITPIPGAPGyvLGVINLRGEVLPVIDLRRLLGLPPTEPR-ERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339977384 614 YALLVDQLIGQHQVVVKNLESNY---RKVPGISAATILGDGSVALIVDVSAL 662
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLglgRVAGYISGATILGDGRVVLILDVEAL 131
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 394-530 1.75e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 95.41  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384  394 DPLTHLVRNSLDHGIELPEKRmesgknvvGNLILSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDDEVG 473
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTPEG--------GRITVTLERDGDHVEITVEDNGPGI---------------------PPEDL 54

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1339977384  474 MLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:smart00387  55 EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 7-99 5.61e-23

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: 93.47  E-value: 5.61e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384    7 DFYQTFFDEADELLADMEQHLLDLApEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGEMQLNTA 86
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELE-KALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 1339977384   87 IINLFLETKDIMQ 99
Cdd:smart00073  80 LLDLLLELVDVLK 92
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-103 7.94e-22

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: 90.13  E-value: 7.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384   5 ISDFYQTFFDEADELLADMEQHLLDLapeaPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARRGeMQLN 84
Cdd:cd00088     1 MEELLELFLEEAEELLEELERALLEL----EDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                          90
                  ....*....|....*....
gi 1339977384  85 TAIINLFLETKDIMQEQLD 103
Cdd:cd00088    76 PELIDLLLDALDALKAELE 94
CheY-binding pfam09078
CheY binding; Members of this family adopt a secondary structure consisting of an open-face ...
 164-226 4.24e-19

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: 81.45  E-value: 4.24e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1339977384 164 RIFLSRLKASEVALLEEELGNLSTLSDVVKGEDRLAATLDGDIAEDDVIAVLCFVIEADQIAF 226
Cdd:pfam09078   1 RIRLSGVSDKDVELLVEELGLLGEVLAQEQAGDSLSVWLETTVSEDDIIAVCCFVVDPDQIVI 63
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 285-346 3.84e-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: 73.04  E-value: 3.84e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1339977384 285 SIRVAVEKVDQLINLVGELVITQSMLAQRSNEL----DPVNHGDLITSMGQLQRNARDLQESVMSI 346
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLeeygGDTLLEELKEALQQLDRLTRELQEAVMKI 66
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 393-530 2.01e-14

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 69.70  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 393 IDPLTHLVRNSLDHGIElpekrmESGKNVVGNLILsaeHQGGNICIEVTDDGAGLNRERIlakaisqgmavnenmtddev 472
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIPPEDL-------------------- 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1339977384 473 gMLIFAPgFSTAEqVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:pfam02518  54 -PRIFEP-FSTAD-KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-78 1.42e-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: 66.61  E-value: 1.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1339977384   7 DFYQTFFDEADELLADMEQHLldlapeapDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDDARR 78
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGEL 64
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
360-530 2.68e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.94  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 360 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDHGielPEKrmesgknvvGNLILSAEHQGGNIC 437
Cdd:COG2205   102 EELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLDNAIKYS---PPG---------GTITISARREGDGVR 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 438 IEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 517
Cdd:COG2205   167 ISVSDNGPGIPEE-ELER--------------------IFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEP 224

                         170
                  ....*....|...
gi 1339977384 518 GTGTTIRILLPLT 530
Cdd:COG2205   225 GGGTTFTVTLPLA 237
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
360-530 1.01e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 69.55  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 360 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDHgielpekrMESGKNVVgnliLSAEHQGGNIC 437
Cdd:COG0642   193 ELFRPLAEEKGIELELDLPDDLPTVrgDPDRLRQV---LLNLLSNAIKY--------TPEGGTVT----VSVRREGDRVR 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 438 IEVTDDGAGlnrerilakaisqgmavnenMTDDEVGMlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQ 517
Cdd:COG0642   258 ISVEDTGPG--------------------IPPEDLER-IFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEP 315

                         170
                  ....*....|...
gi 1339977384 518 GTGTTIRILLPLT 530
Cdd:COG0642   316 GKGTTFTVTLPLA 328
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 360-530 5.59e-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: 64.98  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 360 RLVRDLAGKLGKQVELTLVGSSTEL--DKSLIERIidpLTHLVRNSLDHgielpekrMESGknvvGNLILSAEHQGGNIC 437
Cdd:COG5000   287 ALYEPALKEKDIRLELDLDPDLPEVlaDRDQLEQV---LINLLKNAIEA--------IEEG----GEIEVSTRREDGRVR 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 438 IEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQ 517
Cdd:COG5000   352 IEVSDNGPGIPEE-VLER--------------------IFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRP 405

                         170
                  ....*....|...
gi 1339977384 518 GTGTTIRILLPLT 530
Cdd:COG5000   406 GGGTTFTIRLPLA 418
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 360-530 7.59e-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: 7.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 360 RLVRDLAGKLGKQVELTLVGS--STELDKSLIERIidpLTHLVRNSLDhgielpekRMESGKNvvGNLILSAEHQGGNIC 437
Cdd:COG4191   226 ELLRPRLKARGIEVELDLPPDlpPVLGDPGQLEQV---LLNLLINAID--------AMEEGEG--GRITISTRREGDYVV 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 438 IEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQ 517
Cdd:COG4191   293 ISVRDNGPGIPPE-VLER--------------------IFEPFFTTKPVG---KGTGLGLSISYGIVEKHGGRIEVESEP 348

                         170
                  ....*....|...
gi 1339977384 518 GTGTTIRILLPLT 530
Cdd:COG4191   349 GGGTTFTITLPLA 361
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
362-530 2.23e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 59.86  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 362 VRDLAGK-LGKQVELTLvgsstELDKSLIERIIDP------LTHLVRNSLDHgielpekrMESGknvvGNLILSAE---- 430
Cdd:COG3852   213 VLELLRAeAPKNIRIVR-----DYDPSLPEVLGDPdqliqvLLNLVRNAAEA--------MPEG----GTITIRTRverq 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 431 ------HQGGNICIEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNI 504
Cdd:COG3852   276 vtlgglRPRLYVRIEVIDNGPGIPEE-ILDR--------------------IFEPFFTTKEK-----GTGLGLAIVQKIV 329

                         170       180
                  ....*....|....*....|....*.
gi 1339977384 505 QEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:COG3852   330 EQHGGTIEVESEPGKGTTFRIYLPLE 355
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 385-528 1.20e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 58.00  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 385 DKSLIERIIDPLTHLVRNSLDHGIELPEKRMEsgknvvgnliLSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavn 464
Cdd:PRK11086  427 DEDQVHELITILGNLIENALEAVGGEEGGEIS----------VSLHYRNGWLHCEVSDDGPGIAPDEIDA---------- 486

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1339977384 465 enmtddevgmlIFAPGFSTAEqvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:PRK11086  487 -----------IFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 421-532 7.54e-08

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 55.24  E-value: 7.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 421 VVGNLI------------------LSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDDEVGMLIFAPGFS 482
Cdd:COG3290   285 ILGNLLdnaieaveklpeeerrveLSIRDDGDELVIEVEDSGPGI---------------------PEELLEKIFERGFS 343

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1339977384 483 TAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLA 532
Cdd:COG3290   344 TKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
383-530 3.14e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 53.48  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 383 ELDKSLIERIIDPLT--HLVRNSLDHGIElpekRMESGknvvGNLILSAEHQGGNICIEVTDDGAGLNRERIlaKAISQG 460
Cdd:COG2972   326 EIDEELLDLLIPKLIlqPLVENAIEHGIE----PKEGG----GTIRISIRKEGDRLVITVEDNGVGMPEEKL--EKLLEE 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1339977384 461 MAVNENmtddevgmlifapgfstaeqvtdvsGRGVGMdvvkRNIQEM-------GGHVEIQSKQGTGTTIRILLPLT 530
Cdd:COG2972   396 LSSKGE-------------------------GRGIGL----RNVRERlklyygeEYGLEIESEPGEGTTVTIRIPLE 443
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
286-529 4.30e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 52.63  E-value: 4.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 286 IRVAVEKVDQLINLVGELvitqsmlaqrsneLDpvnhgdlitsMGQLQRNARDLQESVMSIRMMpMEYVFSRFprlvRDL 365
Cdd:COG5002   205 LEIILEEAERLSRLVNDL-------------LD----------LSRLESGELKLEKEPVDLAEL-LEEVVEEL----RPL 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 366 AGKlgKQVELTLVGSSTEL----DKSLIERIidpLTHLVRNSLDHGielPEKrmesgknvvGNLILSAEHQGGNICIEVT 441
Cdd:COG5002   257 AEE--KGIELELDLPEDPLlvlgDPDRLEQV---LTNLLDNAIKYT---PEG---------GTITVSLREEDDQVRISVR 319

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 442 DDGAGlnrerILAKAISQgmavnenmtddevgmlIFAPgFSTAEQVT--DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGT 519
Cdd:COG5002   320 DTGIG-----IPEEDLPR----------------IFER-FYRVDKSRsrETGGTGLGLAIVKHIVEAHGGRIWVESEPGK 377

                         250
                  ....*....|
gi 1339977384 520 GTTIRILLPL 529
Cdd:COG5002   378 GTTFTITLPL 387
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 419-528 4.40e-07

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: 48.60  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 419 KNVVGNLILSAEHQGGnICIEVTDDGAGlNRERILAKAISQGMAVNENMTddevgmlIFAPgFSTAEQVTDVSGRGVGMD 498
Cdd:cd16950     2 KRVLSNLVDNALRYGG-GWVEVSSDGEG-NRTRIQVLDNGPGIAPEEVDE-------LFQP-FYRGDNARGTSGTGLGLA 71

                          90       100       110
                  ....*....|....*....|....*....|
gi 1339977384 499 VVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16950    72 IVQRISDAHGGSLTLANRAGGGLCARIELP 101
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
434-529 4.47e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 53.05  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 434 GNICIEVTDDGAGLNRERILAkaisqgmavnenmtddevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEI 513
Cdd:PRK11360  532 GQVAVSIEDNGCGIDPELLKK---------------------IFDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEV 585

                          90
                  ....*....|....*.
gi 1339977384 514 QSKQGTGTTIRILLPL 529
Cdd:PRK11360  586 ESEPGVGTTFTLYLPI 601
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 350-530 4.55e-07

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: 52.81  E-value: 4.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 350 PMEYVFSRFP--RLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDP------LTHLVRNSLDhgielpekRMESGknv 421
Cdd:COG5805   346 PQAVNKEKENinELIQDVVTLLETEAILHNIQIRLELLDEDPFIYCDEnqikqvFINLIKNAIE--------AMPNG--- 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 422 vGNLILSAEHQGGNICIEVTDDGAGLNRERiLAKaisqgmavnenmtddevgmlIFAPGFSTAEQvtdvsGRGVGMDVVK 501
Cdd:COG5805   415 -GTITIHTEEEDNSVIIRVIDEGIGIPEER-LKK--------------------LGEPFFTTKEK-----GTGLGLMVSY 467

                         170       180
                  ....*....|....*....|....*....
gi 1339977384 502 RNIQEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:COG5805   468 KIIENHNGTIDIDSKVGKGTTFTITLPLS 496
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 433-528 1.96e-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: 46.99  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 433 GGNICIEVTDDGAGLNRErILAKAisqgmavnenmtddevgmliFAPGFSTAEQVtdvSGRGVGMDVVKRNIQEMGGHVE 512
Cdd:cd16919    45 GNYVCLEVSDTGSGMPAE-VLRRA--------------------FEPFFTTKEVG---KGTGLGLSMVYGFVKQSGGHLR 100

                          90
                  ....*....|....*.
gi 1339977384 513 IQSKQGTGTTIRILLP 528
Cdd:cd16919   101 IYSEPGVGTTVRIYLP 116
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 420-529 4.97e-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: 49.59  E-value: 4.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 420 NVVGNLIlSAEHQGGNICIEVTDdgagLNRERILAKAISQGMAVNENMTDdevgmLIFAPGFSTAEQvtdvsGRGVGMDV 499
Cdd:COG5809   386 NLLKNAI-EAMPEGGNITIETKA----EDDDKVVISVTDEGCGIPEERLK-----KLGEPFYTTKEK-----GTGLGLMV 450

                          90       100       110
                  ....*....|....*....|....*....|
gi 1339977384 500 VKRNIQEMGGHVEIQSKQGTGTTIRILLPL 529
Cdd:COG5809   451 SYKIIEEHGGKITVESEVGKGTTFSITLPI 480
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 385-528 1.06e-05

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 48.63  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 385 DKSLIERIidpLTHLVRNSLDHgielpekrmeSGKNVVGNLILSAEHQGGNICIEVTDDGAGLN---RERilakaisqgm 461
Cdd:COG4251   391 DPTLLRQV---FQNLISNAIKY----------SRPGEPPRIEIGAEREGGEWVFSVRDNGIGIDpeyAEK---------- 447

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1339977384 462 avnenmtddevgmlIFAPgFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:COG4251   448 --------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 399-528 1.63e-05

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: 44.20  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 399 LVRNSLD--HGIELPEKRMEsgknvvgnliLSAEHQGGNICIEVTDDGAGLnrerilakaisqgmavnenmtDDEVGMLI 476
Cdd:cd16915     8 LIDNALDalAATGAPNKQVE----------VFLRDEGDDLVIEVRDTGPGI---------------------APELRDKV 56

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1339977384 477 FAPGFSTAEQvtdvSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16915    57 FERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
538-662 2.11e-05

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 44.86  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 538 SVRVADEVFILPLNAVMESLQPRDddLHPLAGGER----VLEVRGEYLPLVELWKVFEVEgAKTEATQGIVVILQSGGRR 613
Cdd:COG0835    12 TFRLGGERYAIPIEKVREILPLPP--ITPVPGAPPwvlgVINLRGRVVPVIDLRALLGLP-PTEDTERTRIIVLEVGGRV 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1339977384 614 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILG----DGSVALIVDVSAL 662
Cdd:COG0835    89 VGLLVDSVSGVVRIDPDDIEPPPELLSGGLAPFITGvaklDDRLILLLDLEKL 141
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
360-529 2.21e-05

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 47.47  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 360 RLVRDLAGKLGKQVELTlVGSSTELDKSLIERIIDPLTHLVRNSLDhgielpekRMESGknvvGNLILSAEHQGGNICIE 439
Cdd:PRK10364  318 QLVSQDANSREIQLRFT-ANDTLPEIQADPDRLTQVLLNLYLNAIQ--------AIGQH----GVISVTASESGAGVKIS 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 440 VTDDGAGLNRERILAkaisqgmavnenmtddevgmlIFAPGFSTAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQSKQGT 519
Cdd:PRK10364  385 VTDSGKGIAADQLEA---------------------IFTPYFTTKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGK 438

                         170
                  ....*....|
gi 1339977384 520 GTTIRILLPL 529
Cdd:PRK10364  439 GATFTLWLPV 448
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 420-529 3.17e-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: 43.64  E-value: 3.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 420 NVVGNLI--------------LSAEHQGGNICIEVTDDGAGLNRERILakaisqgmavnenmtddevgmLIFAPgFSTAE 485
Cdd:cd16922     7 NLLGNAIkfteegevtlrvslEEEEEDGVQLRFSVEDTGIGIPEEQQA---------------------RLFEP-FSQAD 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1339977384 486 QVT--DVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPL 529
Cdd:cd16922    65 SSTtrKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK13557 PRK13557
histidine kinase; Provisional
 267-540 3.27e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 46.97  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 267 AQTGRVEREKPARASEStsIRVAVEKVDQLinlvgelviTQSMLA-QRSNELD--PVNHGDLITSMGQLQRNArdlqesv 343
Cdd:PRK13557  192 LSHPDADRGRMARSVEN--IRAAAERAATL---------TQQLLAfARKQRLEgrVLNLNGLVSGMGELAERT------- 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 344 msirmmpmeyvfsrfprlvrdlagkLGKQVELtlvgsSTELDKSLIERIIDP------LTHLVRNSLDHGIELPEKRMES 417
Cdd:PRK13557  254 -------------------------LGDAVTI-----ETDLAPDLWNCRIDPtqaevaLLNVLINARDAMPEGGRVTIRT 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 418 GKNVVGNLILSAEHQ---GGNICIEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPGFSTAEQVtdvSGRG 494
Cdd:PRK13557  304 RNVEIEDEDLAMYHGlppGRYVSIAVTDTGSGMPPE-ILAR--------------------VMDPFFTTKEEG---KGTG 359

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1339977384 495 VGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLTLAILDGMSVR 540
Cdd:PRK13557  360 LGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFPASDQAENPEQEP 405
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 438-529 6.91e-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: 6.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 438 IEVTDDGAGLNRErILAKaisqgmavnenmtddevgmlIFAPGFSTAEQVTdvsGRGVGMDVVKRNIQEMGGHVEIQSKQ 517
Cdd:cd16943    38 IEVEDTGSGIDPE-ILGR--------------------IFDPFFTTKPVGE---GTGLGLSLSYRIIQKHGGTIRVASVP 93

                          90
                  ....*....|..
gi 1339977384 518 GTGTTIRILLPL 529
Cdd:cd16943    94 GGGTRFTIILPI 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 421-528 1.99e-04

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: 41.12  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 421 VVGNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtddevgmlIFAPGFSTAEQVTDVSGRGVGMDVV 500
Cdd:cd16948    23 QGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPR---------------------VFDKGFTGENGRNFQESTGMGLYLV 81

                          90       100
                  ....*....|....*....|....*...
gi 1339977384 501 KRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16948    82 KKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 396-528 2.81e-04

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 40.60  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 396 LTHLVRNSLDHGIELPEKRMESGknvvgnlILSAEHQGGNICIEVTDDGAGLNRERIlakaisqGMAVNENMTDDEVGMl 475
Cdd:cd16944     9 LTNILKNAAEAIEGRPSDVGEVR-------IRVEADQDGRIVLIVCDNGKGFPREMR-------HRATEPYVTTRPKGT- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1339977384 476 ifapgfstaeqvtdvsgrGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16944    74 ------------------GLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
303-530 4.35e-04

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 42.68  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 303 LVITQSMLAQRSNELDPVNHGDLITSMGQLQRNA-RDLQESVMSIRMMPMEYV--FSRFPRLVRDLAGKLGKQVELTLVG 379
Cdd:COG4585    71 AIKLQLEAARRLLDADPEAAREELEEIRELAREAlAELRRLVRGLRPPALDDLglAAALEELAERLLRAAGIRVELDVDG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 380 SSTELDKSL---IERIIdplTHLVRNSLDHGielpekrmeSGKNVVgnliLSAEHQGGNICIEVTDDGAGLNRERilaka 456
Cdd:COG4585   151 DPDRLPPEVelaLYRIV---QEALTNALKHA---------GATRVT----VTLEVDDGELTLTVRDDGVGFDPEA----- 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1339977384 457 isqgmavnenmtddevgmlifapgfstaeqvtdVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:COG4585   210 ---------------------------------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 492-528 8.14e-04

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 39.23  E-value: 8.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1339977384 492 GRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16921    69 GTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
 396-528 8.98e-04

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


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 40.40  E-value: 8.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 396 LTHLVRNSLDHGIELPEKRMESGKNVVGNLILSAEHqggnICIEVTDDGAGLNReRILAKAISQGMAVNENMTDDEVGML 475
Cdd:cd16929    48 LFELLKNAMRATVESHGDDSDDLPPIKVTVAKGDED----LTIKISDRGGGIPR-EDLARLFSYMYSTAPQPSLDDFSDL 122

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1339977384 476 IfapgfsTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGTGTTIRILLP 528
Cdd:cd16929   123 I------SGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
PRK15347 PRK15347
two component system sensor kinase;
423-530 3.45e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.78  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1339977384 423 GNLILSAEHQGGNICIEVTDDGAGLNRERILAkaisqgmavnenmtddevgmlIFAPGFSTAeqvTDVSGRGVGMDVVKR 502
Cdd:PRK15347  532 GGIRLRVKRHEQQLCFTVEDTGCGIDIQQQQQ---------------------IFTPFYQAD---THSQGTGLGLTIASS 587

                          90       100
                  ....*....|....*....|....*...
gi 1339977384 503 NIQEMGGHVEIQSKQGTGTTIRILLPLT 530
Cdd:PRK15347  588 LAKMMGGELTLFSTPGVGSCFSLVLPLN 615
PRK15347 PRK15347
two component system sensor kinase;
25-74 5.91e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.01  E-value: 5.91e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1339977384  25 QHLLDLAPEAPDA-EQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLD 74
Cdd:PRK15347  844 QSLLLLLAQIEQAvENQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENALE 894
 
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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