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Conserved domains on  [gi|647811513|gb|AIC15214|]
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chemotactic sensor histidine kinase CheA [Nitrososphaera viennensis EN76]

Protein Classification

chemotaxis protein CheA( domain architecture ID 11428864)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
8-542 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 606.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   8 SAYRDLFVQEAHEHVQNMNQALLKLEEDPKSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSS 87
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  88 EMASYLFKCIDTIQEMVD----DENKKVNIEQYLSDLRNPA------------------AVGGGKAASQEGASQQQQQQQ 145
Cdd:COG0643   84 ELIDLLLEALDALRALLDaleaGGEPPADISALLARLDASEeaieevvadeveisppapAALEPAPAAAPPAEAAAAAAE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 146 QHSALPQTIRVKMQDLDALVDLVGELLIAKMRLEQMVG--NTTTDNRVRHTFMSLGRLVSDLQYQTMKLRLVPVEQIFNR 223
Cdd:COG0643  164 AAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEelEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 224 FPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEMPEEREAAGKPQTGTIKLIASKVGDRVM 303
Cdd:COG0643  244 FPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVV 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 304 ITVEDDGRGIDLEKVKAKAIEKKIITKEEADSMSEQDILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIE 383
Cdd:COG0643  324 IEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIE 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 384 TRKGKGTRFTMIIPLSLAIIGGLLVTISDEKYVLPLSSVISTMRVDKKDVKIVHGKEVILFREQVVPLLRTGKSLGIisq 463
Cdd:COG0643  404 SEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGL--- 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647811513 464 qqqkeqqhqQQADEYNHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:COG0643  481 ---------PGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAAL 550
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
8-542 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 606.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   8 SAYRDLFVQEAHEHVQNMNQALLKLEEDPKSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSS 87
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  88 EMASYLFKCIDTIQEMVD----DENKKVNIEQYLSDLRNPA------------------AVGGGKAASQEGASQQQQQQQ 145
Cdd:COG0643   84 ELIDLLLEALDALRALLDaleaGGEPPADISALLARLDASEeaieevvadeveisppapAALEPAPAAAPPAEAAAAAAE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 146 QHSALPQTIRVKMQDLDALVDLVGELLIAKMRLEQMVG--NTTTDNRVRHTFMSLGRLVSDLQYQTMKLRLVPVEQIFNR 223
Cdd:COG0643  164 AAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEelEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 224 FPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEMPEEREAAGKPQTGTIKLIASKVGDRVM 303
Cdd:COG0643  244 FPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVV 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 304 ITVEDDGRGIDLEKVKAKAIEKKIITKEEADSMSEQDILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIE 383
Cdd:COG0643  324 IEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIE 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 384 TRKGKGTRFTMIIPLSLAIIGGLLVTISDEKYVLPLSSVISTMRVDKKDVKIVHGKEVILFREQVVPLLRTGKSLGIisq 463
Cdd:COG0643  404 SEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGL--- 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647811513 464 qqqkeqqhqQQADEYNHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:COG0643  481 ---------PGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAAL 550
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-542 1.35e-93

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 299.72  E-value: 1.35e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   8 SAYRDLFVQEAHEHVQNMNQALLKLEEDPKSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSS 87
Cdd:PRK10547   4 SDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  88 EMASYLFKCIDTIQEMVD--------DEN--------------------------------------------------- 108
Cdd:PRK10547  84 DIINLFLETKDIMQEQLDayktsqepDAAsfeyicqalrqlaleakgetpsavtrlsvvaiqeksepqdesprsqsglri 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 109 -----KKVNIEQYLSDLRN------------------------------------------------------------- 122
Cdd:PRK10547 164 ilsrlKAGEVDLLEEELGNlgtltdvvkgadsleatlpgsvaedditavlcfvieadqitfetavaapqekaeettevve 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 123 -----PAAVGGGKAASQEGASQQQQQQQQHSALPQTIRVKMQDLDALVDLVGELLIAKMRLEQMVGNTttdNRVRH---- 193
Cdd:PRK10547 244 vspkiSVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSEL---DPVNHgdli 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 194 TFMS-LGRLVSDLQYQTMKLRLVPVEQIFNRFPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADH 272
Cdd:PRK10547 321 TSMGqLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 273 AIEMPEEREAAGKPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKVKAKAIEKKIITkeeADSMSEQDILDLLGTPGLST 352
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAV---SENMSDEEVGMLIFAPGFST 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 353 AKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLSLAIIGGLLVTISDEKYVLPLSSVISTMRVDKKD 432
Cdd:PRK10547 478 AEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREED 557

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 433 VKIVHGKEVIL-FREQVVPLL-----------RTGKSLGIisqqqqkeqqhqqqadeynhyltVVIVNKNGKPYGLIVDA 500
Cdd:PRK10547 558 LHPLAGGERVLeVRGEYLPLVelwkvfdvagaKTEATQGI-----------------------VVILQSAGRRYALLVDQ 614

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 647811513 501 FESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:PRK10547 615 LIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 220-397 3.17e-84

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: 259.05  E-value: 3.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 220 IFNRFPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEMPEEREAAGKPQTGTIKLIASKVG 299
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 300 DRVMITVEDDGRGIDLEKVKAKAIEKKIITKEEADSMSEQDILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQ 379
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 647811513 380 VKIETRKGKGTRFTMIIP 397
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 260-399 1.03e-22

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 93.10  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   260 DPLLHMLRNAADHAIEmpeereAAgkPQTGTIKLIASKVGDRVMITVEDDGRGIDLEkvkakaiekkiitkeeadsmseq 339
Cdd:smart00387   4 DRLRQVLSNLLDNAIK------YT--PEGGRITVTLERDGDHVEITVEDNGPGIPPE----------------------- 52

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   340 dILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:smart00387  53 -DLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 405-542 1.95e-16

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: 75.70  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  405 GLLVTISDEKYVLPLSSVISTMRVDK-KDVKIVHG--KEVILFREQVVPLLRTGKSLGIisqqqqkeqqhqqQADEYNHY 481
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPiTPIPGAPGyvLGVINLRGEVLPVIDLRRLLGL-------------PPTEPRER 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647811513  482 LTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSE---ATILGDGKVALILDPARL 542
Cdd:pfam01584  68 TRVVVVEVGGQVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYisgATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
8-542 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 606.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   8 SAYRDLFVQEAHEHVQNMNQALLKLEEDPKSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSS 87
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  88 EMASYLFKCIDTIQEMVD----DENKKVNIEQYLSDLRNPA------------------AVGGGKAASQEGASQQQQQQQ 145
Cdd:COG0643   84 ELIDLLLEALDALRALLDaleaGGEPPADISALLARLDASEeaieevvadeveisppapAALEPAPAAAPPAEAAAAAAE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 146 QHSALPQTIRVKMQDLDALVDLVGELLIAKMRLEQMVG--NTTTDNRVRHTFMSLGRLVSDLQYQTMKLRLVPVEQIFNR 223
Cdd:COG0643  164 AAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEelEDESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNR 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 224 FPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEMPEEREAAGKPQTGTIKLIASKVGDRVM 303
Cdd:COG0643  244 FPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVV 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 304 ITVEDDGRGIDLEKVKAKAIEKKIITKEEADSMSEQDILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIE 383
Cdd:COG0643  324 IEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIE 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 384 TRKGKGTRFTMIIPLSLAIIGGLLVTISDEKYVLPLSSVISTMRVDKKDVKIVHGKEVILFREQVVPLLRTGKSLGIisq 463
Cdd:COG0643  404 SEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRLGELLGL--- 480

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647811513 464 qqqkeqqhqQQADEYNHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:COG0643  481 ---------PGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAAL 550
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-542 1.35e-93

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 299.72  E-value: 1.35e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   8 SAYRDLFVQEAHEHVQNMNQALLKLEEDPKSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSS 87
Cdd:PRK10547   4 SDFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  88 EMASYLFKCIDTIQEMVD--------DEN--------------------------------------------------- 108
Cdd:PRK10547  84 DIINLFLETKDIMQEQLDayktsqepDAAsfeyicqalrqlaleakgetpsavtrlsvvaiqeksepqdesprsqsglri 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 109 -----KKVNIEQYLSDLRN------------------------------------------------------------- 122
Cdd:PRK10547 164 ilsrlKAGEVDLLEEELGNlgtltdvvkgadsleatlpgsvaedditavlcfvieadqitfetavaapqekaeettevve 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 123 -----PAAVGGGKAASQEGASQQQQQQQQHSALPQTIRVKMQDLDALVDLVGELLIAKMRLEQMVGNTttdNRVRH---- 193
Cdd:PRK10547 244 vspkiSVPPVLKLAAEQAPAGRVEREKTARSSESTSIRVAVEKVDQLINLVGELVITQSMLAQRSSEL---DPVNHgdli 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 194 TFMS-LGRLVSDLQYQTMKLRLVPVEQIFNRFPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADH 272
Cdd:PRK10547 321 TSMGqLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 273 AIEMPEEREAAGKPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKVKAKAIEKKIITkeeADSMSEQDILDLLGTPGLST 352
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAV---SENMSDEEVGMLIFAPGFST 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 353 AKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLSLAIIGGLLVTISDEKYVLPLSSVISTMRVDKKD 432
Cdd:PRK10547 478 AEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQPREED 557

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 433 VKIVHGKEVIL-FREQVVPLL-----------RTGKSLGIisqqqqkeqqhqqqadeynhyltVVIVNKNGKPYGLIVDA 500
Cdd:PRK10547 558 LHPLAGGERVLeVRGEYLPLVelwkvfdvagaKTEATQGI-----------------------VVILQSAGRRYALLVDQ 614

                        650       660       670       680
                 ....*....|....*....|....*....|....*....|..
gi 647811513 501 FESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:PRK10547 615 LIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 220-397 3.17e-84

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: 259.05  E-value: 3.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 220 IFNRFPRMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEMPEEREAAGKPQTGTIKLIASKVG 299
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 300 DRVMITVEDDGRGIDLEKVKAKAIEKKIITKEEADSMSEQDILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQ 379
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 647811513 380 VKIETRKGKGTRFTMIIP 397
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 400-542 8.43e-29

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: 110.73  E-value: 8.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 400 LAIIGGLLVTISDEKYVLPLSSVISTMRVDKKDVKIVHG-KEVILFREQVVPLLRTGKSLGIisqqqqkeqqhqQQADEY 478
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGgKEVINVRGELLPLVRLGELFNV------------RGENEE 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647811513 479 NHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSEATILGDGKVALILDPARL 542
Cdd:cd00731   69 PDEGVVVVVRTGGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 260-399 1.03e-22

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 93.10  E-value: 1.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   260 DPLLHMLRNAADHAIEmpeereAAgkPQTGTIKLIASKVGDRVMITVEDDGRGIDLEkvkakaiekkiitkeeadsmseq 339
Cdd:smart00387   4 DRLRQVLSNLLDNAIK------YT--PEGGRITVTLERDGDHVEITVEDNGPGIPPE----------------------- 52

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   340 dILDLLGTPGLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:smart00387  53 -DLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 7-105 3.10e-20

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: 85.51  E-value: 3.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   7 KSAYRDLFVQEAHEHVQNMNQALLKLEEDpkskEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRkDEERMS 86
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELEDA----EDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALR-DGLEVT 75

                         90
                 ....*....|....*....
gi 647811513  87 SEMASYLFKCIDTIQEMVD 105
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 10-101 6.43e-19

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


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 81.53  E-value: 6.43e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513    10 YRDLFVQEAHEHVQNMNQALLKLEEDPKSKEhLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELFDKFRKDEERMSSEM 89
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKALDAQD-VNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDL 80

                           90
                   ....*....|..
gi 647811513    90 ASYLFKCIDTIQ 101
Cdd:smart00073  81 LDLLLELVDVLK 92
CheW smart00260
Two component signalling adaptor domain;
393-542 3.02e-18

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 81.13  E-value: 3.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   393 TMIIPLSLAIIggllvtiSDEKYVLPLSSVISTMRVDKKDV---KIVHGKEVILFREQVVPLLRTGKSLGIisqqqqkeq 469
Cdd:smart00260   1 TIRLPLTFAIG-------KDETYAIPIAAVREILRPPPITPipgAPGYVLGVINLRGEVLPVVDLRRLLGL--------- 64

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 647811513   470 qhqqQADEYNHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSE----ATILGDGKVALILDPARL 542
Cdd:smart00260  65 ----PPEPPTDETRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPPPPVSLSNAPgisgATILGDGRVVLILDVDKL 137
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 405-542 1.95e-16

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: 75.70  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  405 GLLVTISDEKYVLPLSSVISTMRVDK-KDVKIVHG--KEVILFREQVVPLLRTGKSLGIisqqqqkeqqhqqQADEYNHY 481
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPiTPIPGAPGyvLGVINLRGEVLPVIDLRRLLGL-------------PPTEPRER 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 647811513  482 LTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSE---ATILGDGKVALILDPARL 542
Cdd:pfam01584  68 TRVVVVEVGGQVVGLLVDEVIGVLEIVIKQIEPPLGLGRVAGYisgATILGDGRVVLILDVEAL 131
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 402-542 5.99e-16

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: 74.62  E-value: 5.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 402 IIGGLLVTISDEKYVLPLSSVISTMRVDKKDVKI---VHGKEVILFREQVVPLLRTGKSLGIisqqqqkeqqhqQQADEY 478
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITRVPnapDYVLGVINLRGEILPVIDLRRLFGL------------EAAEPD 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 647811513 479 NHYLTVVIVNKNGKPYGLIVDAFESKQEIVVKRLDSSSAPSSVSSE----ATILGDGKVALILDPARL 542
Cdd:cd00588   69 TDETRIVVVEVGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGSSNAPgisgATILGDGRVVLILDVDKL 136
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 260-398 4.24e-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: 71.25  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513  260 DPLLHMLRNAADHAIEmpeereAAGKPQTGTIKLiasKVGDRVMITVEDDGRGIDlekvkakaiekkiitkeeadsmseQ 339
Cdd:pfam02518   4 LRLRQVLSNLLDNALK------HAAKAGEITVTL---SEGGELTLTVEDNGIGIP------------------------P 50

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 647811513  340 DILDLLGTPGLSTAKqvTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPL 398
Cdd:pfam02518  51 EDLPRIFEPFSTADK--RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPL 107
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 10-102 1.58e-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: 65.84  E-value: 1.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513   10 YRDLFVQEAHEHVQNMNQALlkleedpkSKEHLDSAFRSAHTLKGMAATMGYDQIKELCKAIEELfdkFRKDEERMSSEM 89
Cdd:pfam01627   2 LLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDPEL 70

                          90
                  ....*....|...
gi 647811513   90 ASYLFKCIDTIQE 102
Cdd:pfam01627  71 LEALRDLLEALRA 83
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
198-399 3.69e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.17  E-value: 3.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 198 LGRLVSDL------QYQTMKLRLVPV--EQIFNRFPRMIRDLSSSQGKSLKLEIEGLGIEL--DRTVLDAItdpLLHMLR 267
Cdd:COG2205   66 LLRLIEDLldlsrlESGKLSLELEPVdlAELLEEAVEELRPLAEEKGIRLELDLPPELPLVyaDPELLEQV---LANLLD 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 268 NAADHAiempeereaagkPQTGTIKLIASKVGDRVMITVEDDGRGIDlekvkakaiekkiitkeeadsmseQDILDLLGT 347
Cdd:COG2205  143 NAIKYS------------PPGGTITISARREGDGVRISVSDNGPGIP------------------------EEELERIFE 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 647811513 348 PgLSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:COG2205  187 R-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
198-399 1.86e-12

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 68.40  E-value: 1.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 198 LGRLVSDL--------QYQTMKLRLVPVEQIFNRFPRMIRDLSSSQGKSLKLEIEG--LGIELDRTVLDAItdpLLHMLR 267
Cdd:COG0642  157 LLRLINDLldlsrleaGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDdlPTVRGDPDRLRQV---LLNLLS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 268 NAADHAiempeereaagkPQTGTIKLIASKVGDRVMITVEDDGRGIDlekvkakaiekkiitkeeadsmseQDILDLLGT 347
Cdd:COG0642  234 NAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPGIP------------------------PEDLERIFE 277

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 647811513 348 PGlSTAKQVTDISGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:COG0642  278 PF-FRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
198-398 8.12e-11

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 64.04  E-value: 8.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 198 LGRLVSDLQYQT----MKLRLVPVEQIFNRFPRMIRDLSSSQGKSLKLEI-EGL-GIELDRtvlDAITDPLLHMLRNAAd 271
Cdd:PRK10364 286 LNRVVSELLELVkpthLALQAVDLNDLINHSLQLVSQDANSREIQLRFTAnDTLpEIQADP---DRLTQVLLNLYLNAI- 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 272 HAIempeereaagkPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKvkakaiekkiitkeeadsmseqdiLDLLGTPGLS 351
Cdd:PRK10364 362 QAI-----------GQHGVISVTASESGAGVKISVTDSGKGIAADQ------------------------LEAIFTPYFT 406

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 647811513 352 TAKQvtdisGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPL 398
Cdd:PRK10364 407 TKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 197-399 3.42e-10

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: 62.29  E-value: 3.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 197 SLGRLVSD-LQY---QTMKLRLVPVEQIFNRfprmIRDLSSSQGKSLKLEIEglgIELDRTVLDAITDP------LLHML 266
Cdd:COG5000  254 RLKRIVDEfLDFarlPEPQLEPVDLNELLRE----VLALYEPALKEKDIRLE---LDLDPDLPEVLADRdqleqvLINLL 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 267 RNAADhAIEmpeereaagkpQTGTIKLIASKVGDRVMITVEDDGRGIDlEKVKAKAIEKKIITKEEadsmseqdildllG 346
Cdd:COG5000  327 KNAIE-AIE-----------EGGEIEVSTRREDGRVRIEVSDNGPGIP-EEVLERIFEPFFTTKPK-------------G 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 647811513 347 TP-GLSTAKQVtdisgrgvgmdvvfsqIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:COG5000  381 TGlGLAIVKKI----------------VEEHGGTIELESRPGGGTTFTIRLPLA 418
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 230-399 3.69e-10

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 61.74  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 230 DLSSSQGKSLKLEIEglgIELDRTVLDAITDP------LLHMLRNAADhAieMPEEREaagkpqtGTIKLIASKVGDRVM 303
Cdd:COG4191  226 ELLRPRLKARGIEVE---LDLPPDLPPVLGDPgqleqvLLNLLINAID-A--MEEGEG-------GRITISTRREGDYVV 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 304 ITVEDDGRGIDlekvkakaiekkiitkeeadsmseQDILDLLGTPGLSTaKQVTDisGRGVGMDVVFSQIEAVGGQVKIE 383
Cdd:COG4191  293 ISVRDNGPGIP------------------------PEVLERIFEPFFTT-KPVGK--GTGLGLSISYGIVEKHGGRIEVE 345

                        170
                 ....*....|....*.
gi 647811513 384 TRKGKGTRFTMIIPLS 399
Cdd:COG4191  346 SEPGGGTTFTITLPLA 361
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 268-401 3.93e-10

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 61.79  E-value: 3.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 268 NAADHAIEMPEEReaagkpqtGTIKLIASKVGDRVMITVEDDGRGIDlEKVKAKAIEKKIITKEEAdsmseqdildllgt 347
Cdd:COG3290  292 NAIEAVEKLPEEE--------RRVELSIRDDGDELVIEVEDSGPGIP-EELLEKIFERGFSTKLGE-------------- 348

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 647811513 348 pglstakqvtdisGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLSLA 401
Cdd:COG3290  349 -------------GRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 262-398 2.66e-09

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: 54.74  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 262 LLHMLRNAAdHAIEmpeEReaagkpqtGTIKLIASKVGDRVMITVEDDGRGIDLEkvkakaIEKKIITKeeadsmseqdi 341
Cdd:cd16943    8 LLNLLVNAA-QAME---GR--------GRITIRTWAHVDQVLIEVEDTGSGIDPE------ILGRIFDP----------- 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 647811513 342 ldllgtpgLSTAKQVTDisGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPL 398
Cdd:cd16943   59 --------FFTTKPVGE--GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
248-399 4.26e-08

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 55.24  E-value: 4.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 248 IELDRtvlDAITDPLLHMLRNAADHaieMPEEreaagkpqtGTIKLIASKV----------GDRVMITVEDDGRGIDlek 317
Cdd:COG3852  238 VLGDP---DQLIQVLLNLVRNAAEA---MPEG---------GTITIRTRVErqvtlgglrpRLYVRIEVIDNGPGIP--- 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 318 vkakaiekkiitkeeadsmseQDILDLLGTPGLSTaKQvtdiSGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIP 397
Cdd:COG3852  300 ---------------------EEILDRIFEPFFTT-KE----KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLP 353


                 ..
gi 647811513 398 LS 399
Cdd:COG3852  354 LE 355
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 299-397 1.07e-07

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 50.46  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 299 GDRVMITVEDDGRGIDlEKVKAKAIEKKIITKEEAdsmseqdildllgtpglstakqvtdiSGRGVGMDVVFSQIEAVGG 378
Cdd:cd16919   45 GNYVCLEVSDTGSGMP-AEVLRRAFEPFFTTKEVG--------------------------KGTGLGLSMVYGFVKQSGG 97

                         90
                 ....*....|....*....
gi 647811513 379 QVKIETRKGKGTRFTMIIP 397
Cdd:cd16919   98 HLRIYSEPGVGTTVRIYLP 116
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
198-399 2.33e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 53.02  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 198 LGRLVSDL------QYQTMKLRLVPV------EQIFNRFprmiRDLSSSQGKSLKLEI--EGLGIELDRTVLDAItdpLL 263
Cdd:COG5002  215 LSRLVNDLldlsrlESGELKLEKEPVdlaellEEVVEEL----RPLAEEKGIELELDLpeDPLLVLGDPDRLEQV---LT 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 264 HMLRNAADHAiempeereaagkPQTGTIKLIASKVGDRVMITVEDDGRGIDlekvkAKAIEKkiITK-----EEADSMSE 338
Cdd:COG5002  288 NLLDNAIKYT------------PEGGTITVSLREEDDQVRISVRDTGIGIP-----EEDLPR--IFErfyrvDKSRSRET 348

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 647811513 339 QdildllGTP-GLSTAKQVtdisgrgvgmdvvfsqIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:COG5002  349 G------GTGlGLAIVKHI----------------VEAHGGRIWVESEPGKGTTFTITLPLA 388
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 153-212 3.03e-07

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: 47.62  E-value: 3.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 647811513  153 TIRVKMQDLDALVDLVGELLIAKMRLEQMV------GNTTTDNRVRHTFMSLGRLVSDLQYQTMKL 212
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLerleeyGGDTLLEELKEALQQLDRLTRELQEAVMKI 66
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 281-397 1.23e-06

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 51.07  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 281 EAAGKPQTGTIKLIASKVGDRVMITVEDDGRGIDlekvkakaiekkiitKEEADSMSEQdildllgtpGLSTAKqvtdiS 360
Cdd:PRK11086 447 EAVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIA---------------PDEIDAIFDK---------GYSTKG-----S 497

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 647811513 361 GRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIP 397
Cdd:PRK11086 498 NRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 265-397 2.86e-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: 46.13  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 265 MLRNAADHAIEMPEereaagkpQTGTIKLIASKVGDRVMITVEDDGRGIDLEKvkakaiekkiitkeeADSMSEQdildl 344
Cdd:cd16915    8 LIDNALDALAATGA--------PNKQVEVFLRDEGDDLVIEVRDTGPGIAPEL---------------RDKVFER----- 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 647811513 345 lgtpGLSTAKQvtdiSGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIP 397
Cdd:cd16915   60 ----GVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 281-400 3.09e-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: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 281 EAAGKPQTGTIKlIASKVGDRVMITVEDDGRGIDLEKvkakaiekkiitkeeadsmseqdiLDLLGTPGLSTAKQvtdis 360
Cdd:COG5809  393 EAMPEGGNITIE-TKAEDDDKVVISVTDEGCGIPEER------------------------LKKLGEPFYTTKEK----- 442

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 647811513 361 GRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLSL 400
Cdd:COG5809  443 GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKL 482
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 262-399 3.64e-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: 49.73  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 262 LLHMLRNAADhaiEMPEEreaagkpqtGTIKLIASKVGDRVMITVEDDGRGIDlekvkakaiekkiitkeeadsmseQDI 341
Cdd:COG5805  400 FINLIKNAIE---AMPNG---------GTITIHTEEEDNSVIIRVIDEGIGIP------------------------EER 443

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 647811513 342 LDLLGTPGLSTAKQvtdisGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIPLS 399
Cdd:COG5805  444 LKKLGEPFFTTKEK-----GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
226-398 1.27e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 46.92  E-value: 1.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 226 RMIRDLSSSQGKSLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAiempeereaagkpQTGTIKLIASKVGDRVMIT 305
Cdd:COG4585  131 ELAERLLRAAGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHA-------------GATRVTVTLEVDDGELTLT 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 306 VEDDGRGIDLEKVKakaiekkiitkeeadsmseqdildllgtpglstakqvtdisGRGVGMDVVFSQIEAVGGQVKIETR 385
Cdd:COG4585  198 VRDDGVGFDPEAAP-----------------------------------------GGGLGLRGMRERAEALGGTLTIGSA 236

                        170
                 ....*....|...
gi 647811513 386 KGKGTRFTMIIPL 398
Cdd:COG4585  237 PGGGTRVRATLPL 249
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
268-398 4.25e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 46.16  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 268 NAADHAIEmpeereaaGKPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKVKAkaiekkiitkeeadsmseqdILDLLGT 347
Cdd:COG2972  347 NAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEK--------------------LLEELSS 398

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 647811513 348 PGlstakqvtdiSGRGVGMDVVFSQIEA---VGGQVKIETRKGKGTRFTMIIPL 398
Cdd:COG2972  399 KG----------EGRGIGLRNVRERLKLyygEEYGLEIESEPGEGTTVTIRIPL 442
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 189-399 5.81e-05

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 45.67  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 189 NRVRhtfmSLGRlVSDLQYQTMKLRLVPVEQIFNRFPRMIRDLSSSQGKSLKLEIEGLGIELDRTVldaitdPL---LH- 264
Cdd:COG3920  338 NRIQ----ALAL-VHELLYQSEDWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPDVELPADAAV------PLgliLNe 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 265 MLRNAADHAiempeereaAGKPQTGTIKLIASKVGDRVMITVEDDGRGIDlekvkakaiekkiitkeeadsmseqdildl 344
Cdd:COG3920  407 LVTNALKHA---------FLSGEGGRIRVSWRREDGRLRLTVSDNGVGLP------------------------------ 447

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 647811513 345 lgtpglstaKQVTDISGRGVGMDVVFSQIEAVGGQVKIETrkGKGTRFTMIIPLS 399
Cdd:COG3920  448 ---------EDVDPPARKGLGLRLIRALVRQLGGTLELDR--PEGTRVRITFPLA 491
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 219-314 1.42e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 42.02  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 219 QIFNRFPRMIRDLSSSQGksLKLEIEGLGIELDRTVLDAITDPLLHMLRNAADHAIEmpeEREaagkpqTGTIKLIASKV 298
Cdd:cd16951    3 EYINRIASAINAIHAVGD--IRINITGDTGPVSSEVATAIGLVVNELLQNALKHAFS---DRE------GGTITIRSVVD 71

                         90
                 ....*....|....*.
gi 647811513 299 GDRVMITVEDDGRGID 314
Cdd:cd16951   72 GDYLRITVIDDGVGLP 87
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 257-397 2.96e-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: 40.21  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 257 AITDPLLHMLRNAADHAiempEEREAaGKPQtGTIKLIASKVGdRVMITVEDDGRGIDLEkVKAKAIEKKIITKEEadsm 336
Cdd:cd16944    4 QISQVLTNILKNAAEAI----EGRPS-DVGE-VRIRVEADQDG-RIVLIVCDNGKGFPRE-MRHRATEPYVTTRPK---- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 647811513 337 seqdildllgtpglstakqvtdisGRGVGMDVVFSQIEAVGGQVKIETRKGKGTRFTMIIP 397
Cdd:cd16944   72 ------------------------GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 262-397 2.09e-03

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 37.94  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 262 LLHMLRNAADHAIEMpeereaaGKPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKVkaKAIEKKIITKEEADSMSEQDi 341
Cdd:cd16953    1 LGQVLRNLIGNAISF-------SPPDTGRITVSAMPTGKMVTISVEDEGPGIPQEKL--ESIFDRFYTERPANEAFGQH- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 647811513 342 ldllGTPGLSTAKQVtdisgrgvgmdvvfsqIEAVGGQVKIETR----KGKGTRFTMIIP 397
Cdd:cd16953   71 ----SGLGLSISRQI----------------IEAHGGISVAENHnqpgQVIGARFTVQLP 110
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
265-319 3.01e-03

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 37.97  E-value: 3.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 647811513 265 MLRNAADHAiempeereaAGKPQTGTIKLIASKVGDRVMITVEDDGRGIDLEKVK 319
Cdd:COG2172   42 AVTNAVRHA---------YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLP 87
 
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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