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Conserved domains on  [gi|515631512|ref|WP_017064112|]
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MULTISPECIES: chemotaxis protein CheA [Vibrio]

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];
6-729 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 665.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   6 DEDILQDFLVEAGEILELLSEQLVELENNPDDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  86 SGLMDTMLQALDTVNVQFRAVQDQEPLVPADQSLLDELHrlckpesadevAPVEAPAPIIPEPVVAAPEPVIAPEPtaes 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARLD-----------ASEEAIEEVVADEVEISPPAPAALEP---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 166 sninassvddisedeferlldelhgkggsptapsaptpppapaapqsvadsgditddefeklldelhgagksptaasstp 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 246 pppptppaapvsamsegddlmtdeefeklldqlhgsgngpsieeldaatkpaevkavapqaapkpaapvavkaEPKPSAP 325
Cdd:COG0643  148 -------------------------------------------------------------------------APAAAPP 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 326 AKAEVKVPAKKQQAEATVRVDTSTLDTIMNMVGELVLVRNRLVSLGLNSNDE---EMSKAVSNLDVVTADLQGAVMKTRM 402
Cdd:COG0643  155 AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQLSRLTRELQDGVMRLRM 234

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 403 QPIKKVFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILS 482
Cdd:COG0643  235 VPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLS 314

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAASRLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAIN 562
Cdd:COG0643  315 AYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIE 394

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFALPLASVNEIFHLDLSRTNVVDGQLTIIVRDKSIPLFYL 642
Cdd:COG0643  395 ALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRL 474

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 643 QNWLAPKAGIVElrKGHGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPDLLK 722
Cdd:COG0643  475 GELLGLPGAEPE--GERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552


                 ....*..
gi 515631512 723 QYAAASR 729
Cdd:COG0643  553 SARARAR 559
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-729 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 665.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   6 DEDILQDFLVEAGEILELLSEQLVELENNPDDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  86 SGLMDTMLQALDTVNVQFRAVQDQEPLVPADQSLLDELHrlckpesadevAPVEAPAPIIPEPVVAAPEPVIAPEPtaes 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARLD-----------ASEEAIEEVVADEVEISPPAPAALEP---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 166 sninassvddisedeferlldelhgkggsptapsaptpppapaapqsvadsgditddefeklldelhgagksptaasstp 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 246 pppptppaapvsamsegddlmtdeefeklldqlhgsgngpsieeldaatkpaevkavapqaapkpaapvavkaEPKPSAP 325
Cdd:COG0643  148 -------------------------------------------------------------------------APAAAPP 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 326 AKAEVKVPAKKQQAEATVRVDTSTLDTIMNMVGELVLVRNRLVSLGLNSNDE---EMSKAVSNLDVVTADLQGAVMKTRM 402
Cdd:COG0643  155 AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQLSRLTRELQDGVMRLRM 234

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 403 QPIKKVFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILS 482
Cdd:COG0643  235 VPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLS 314

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAASRLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAIN 562
Cdd:COG0643  315 AYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIE 394

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFALPLASVNEIFHLDLSRTNVVDGQLTIIVRDKSIPLFYL 642
Cdd:COG0643  395 ALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRL 474

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 643 QNWLAPKAGIVElrKGHGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPDLLK 722
Cdd:COG0643  475 GELLGLPGAEPE--GERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552


                 ....*..
gi 515631512 723 QYAAASR 729
Cdd:COG0643  553 SARARAR 559
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-720 2.93e-116

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 364.82  E-value: 2.93e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   8 DILQDFLVEAGEILELLSEQLVELENNPDDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVTSG 87
Cdd:PRK10547   5 DFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  88 LMDTMLQALDTVNVQFRAVQD-QEPLVPADQSLLDELHRLckpesADEVAPVEAPAPIIPEPVVAAPEPVIAPEPTAESS 166
Cdd:PRK10547  85 IINLFLETKDIMQEQLDAYKTsQEPDAASFEYICQALRQL-----ALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 167 NINASsVDDISEDEFERLLDELHGKGgsptapsaptpppapaapqSVADSGDiTDDEFEKLLDelhgagksptaasstpp 246
Cdd:PRK10547 160 GLRII-LSRLKAGEVDLLEEELGNLG-------------------TLTDVVK-GADSLEATLP----------------- 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 247 ppptppaapvSAMSEgDDLMTDEEFEKLLDQLHgsgngpSIEELDAATKPAEVKAVAPQAAPKPAAPVAVKAEPKPSAPA 326
Cdd:PRK10547 202 ----------GSVAE-DDITAVLCFVIEADQIT------FETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAG 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 327 KAEVKVPAKKqqAEAT-VRVDTSTLDTIMNMVGELVLVRNRLV--SLGLN-SNDEEMSKAVSNLDVVTADLQGAVMKTRM 402
Cdd:PRK10547 265 RVEREKTARS--SESTsIRVAVEKVDQLINLVGELVITQSMLAqrSSELDpVNHGDLITSMGQLQRNARDLQESVMSIRM 342

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 403 QPIKKVFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILS 482
Cdd:PRK10547 343 MPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILS 422

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAasrLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAIN 562
Cdd:PRK10547 423 AEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQ 499

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFALPLASVNEIFH---LDLSrtNVVDGQLTIIVRDKSIPL 639
Cdd:PRK10547 500 EMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQpreEDLH--PLAGGERVLEVRGEYLPL 577

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 640 FYLQNWLAPKAGIVELRKghGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPD 719
Cdd:PRK10547 578 VELWKVFDVAGAKTEATQ--GIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSA 655


                 .
gi 515631512 720 L 720
Cdd:PRK10547 656 L 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 408-585 3.40e-86

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: 269.07  E-value: 3.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 408 VFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILSASQEG 487
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 488 DHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAASRLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAINTLNGS 567
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 515631512 568 IDIDSEMGQGTKITIKVP 585
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
581-721 4.11e-23

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 95.77  E-value: 4.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   581 TIKVPLTLAILPTLMvgvaghpFALPLASVNEIFHLD-LSR--TNVVDGQLTIIVRDKSIPLFYLQNWLAPKAgivELRK 657
Cdd:smart00260   1 TIRLPLTFAIGKDET-------YAIPIAAVREILRPPpITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPP---EPPT 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631512   658 GHGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKL----LQGTPGMAGATITSDGHIALILDVPDLL 721
Cdd:smart00260  71 DETRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPPppvsLSNAPGISGATILGDGRVVLILDVDKLL 138
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 594-720 1.25e-19

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: 85.33  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  594 LMVGVAGHPFALPLASVNEIFHLD-LSRTNVVDGQL--TIIVRDKSIPLFYLQNWLAPKAgivELRKGHGHVVIVQLGSQ 670
Cdd:pfam01584   2 LLFRLGGETFAIPISKVREILRPPpITPIPGAPGYVlgVINLRGEVLPVIDLRRLLGLPP---TEPRERTRVVVVEVGGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515631512  671 RVGFVVDTLIGQEEVVIKPLDKLLQGTPG---MAGATITSDGHIALILDVPDL 720
Cdd:pfam01584  79 VVGLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-729 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 665.34  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   6 DEDILQDFLVEAGEILELLSEQLVELENNPDDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  86 SGLMDTMLQALDTVNVQFRAVQDQEPLVPADQSLLDELHrlckpesadevAPVEAPAPIIPEPVVAAPEPVIAPEPtaes 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARLD-----------ASEEAIEEVVADEVEISPPAPAALEP---- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 166 sninassvddisedeferlldelhgkggsptapsaptpppapaapqsvadsgditddefeklldelhgagksptaasstp 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 246 pppptppaapvsamsegddlmtdeefeklldqlhgsgngpsieeldaatkpaevkavapqaapkpaapvavkaEPKPSAP 325
Cdd:COG0643  148 -------------------------------------------------------------------------APAAAPP 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 326 AKAEVKVPAKKQQAEATVRVDTSTLDTIMNMVGELVLVRNRLVSLGLNSNDE---EMSKAVSNLDVVTADLQGAVMKTRM 402
Cdd:COG0643  155 AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQLSRLTRELQDGVMRLRM 234

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 403 QPIKKVFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILS 482
Cdd:COG0643  235 VPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLS 314

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAASRLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAIN 562
Cdd:COG0643  315 AYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIE 394

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFALPLASVNEIFHLDLSRTNVVDGQLTIIVRDKSIPLFYL 642
Cdd:COG0643  395 ALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEGREVIRLRGELLPLVRL 474

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 643 QNWLAPKAGIVElrKGHGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPDLLK 722
Cdd:COG0643  475 GELLGLPGAEPE--GERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552


                 ....*..
gi 515631512 723 QYAAASR 729
Cdd:COG0643  553 SARARAR 559
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-720 2.93e-116

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 364.82  E-value: 2.93e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   8 DILQDFLVEAGEILELLSEQLVELENNPDDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVTSG 87
Cdd:PRK10547   5 DFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  88 LMDTMLQALDTVNVQFRAVQD-QEPLVPADQSLLDELHRLckpesADEVAPVEAPAPIIPEPVVAAPEPVIAPEPTAESS 166
Cdd:PRK10547  85 IINLFLETKDIMQEQLDAYKTsQEPDAASFEYICQALRQL-----ALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 167 NINASsVDDISEDEFERLLDELHGKGgsptapsaptpppapaapqSVADSGDiTDDEFEKLLDelhgagksptaasstpp 246
Cdd:PRK10547 160 GLRII-LSRLKAGEVDLLEEELGNLG-------------------TLTDVVK-GADSLEATLP----------------- 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 247 ppptppaapvSAMSEgDDLMTDEEFEKLLDQLHgsgngpSIEELDAATKPAEVKAVAPQAAPKPAAPVAVKAEPKPSAPA 326
Cdd:PRK10547 202 ----------GSVAE-DDITAVLCFVIEADQIT------FETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAG 264

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 327 KAEVKVPAKKqqAEAT-VRVDTSTLDTIMNMVGELVLVRNRLV--SLGLN-SNDEEMSKAVSNLDVVTADLQGAVMKTRM 402
Cdd:PRK10547 265 RVEREKTARS--SESTsIRVAVEKVDQLINLVGELVITQSMLAqrSSELDpVNHGDLITSMGQLQRNARDLQESVMSIRM 342

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 403 QPIKKVFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILS 482
Cdd:PRK10547 343 MPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILS 422

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAasrLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAIN 562
Cdd:PRK10547 423 AEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQ 499

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFALPLASVNEIFH---LDLSrtNVVDGQLTIIVRDKSIPL 639
Cdd:PRK10547 500 EMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQpreEDLH--PLAGGERVLEVRGEYLPL 577

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 640 FYLQNWLAPKAGIVELRKghGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPD 719
Cdd:PRK10547 578 VELWKVFDVAGAKTEATQ--GIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDVSA 655


                 .
gi 515631512 720 L 720
Cdd:PRK10547 656 L 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 408-585 3.40e-86

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: 269.07  E-value: 3.40e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 408 VFGRFPRVVRDLARSLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPNDRVAAGKSQTGKVILSASQEG 487
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 488 DHIELAIVDDGGGMDPDKLRAIAVKRGLMDEDAASRLSNKECFNLIFAPGFSSKEQISDISGRGVGMDVVKTAINTLNGS 567
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 515631512 568 IDIDSEMGQGTKITIKVP 585
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 588-720 7.45e-37

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: 134.61  E-value: 7.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 588 LAILPTLMVGVAGHPFALPLASVNEIFHLDLSRTNVVDG-QLTIIVRDKSIPLFYLQNWLapKAGIVELRKGHGHVVIVQ 666
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGgKEVINVRGELLPLVRLGELF--NVRGENEEPDEGVVVVVR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515631512 667 LGSQRVGFVVDTLIGQEEVVIKPLDKLLQGTPGMAGATITSDGHIALILDVPDL 720
Cdd:cd00731   79 TGGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
581-721 4.11e-23

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 95.77  E-value: 4.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   581 TIKVPLTLAILPTLMvgvaghpFALPLASVNEIFHLD-LSR--TNVVDGQLTIIVRDKSIPLFYLQNWLAPKAgivELRK 657
Cdd:smart00260   1 TIRLPLTFAIGKDET-------YAIPIAAVREILRPPpITPipGAPGYVLGVINLRGEVLPVVDLRRLLGLPP---EPPT 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515631512   658 GHGHVVIVQLGSQRVGFVVDTLIGQEEVVIKPLDKL----LQGTPGMAGATITSDGHIALILDVPDLL 721
Cdd:smart00260  71 DETRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPPppvsLSNAPGISGATILGDGRVVLILDVDKLL 138
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 445-587 9.38e-22

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 90.79  E-value: 9.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   445 ALADPLIHLVRNSVDHGIEmpndrvAAGksQTGKVILSASQEGDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrl 524
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIK------YTP--EGGRITVTLERDGDHVEITVEDNGPGIPPEDL------------------ 54

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631512   525 snkecfNLIFAPGFSSKEQISDISGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:smart00387  55 ------EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 590-720 2.90e-20

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: 87.33  E-value: 2.90e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 590 ILPTLMVGVAGHPFALPLASVNEIFHLDLSR---TNVVDGQLTIIVRDKSIPLFYLQNWLAPKAGivELRKGHGHVVIVQ 666
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITrvpNAPDYVLGVINLRGEILPVIDLRRLFGLEAA--EPDTDETRIVVVE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515631512 667 LGSQRVGFVVDTLIGQEEVVIKPLDKLLQGT----PGMAGATITSDGHIALILDVPDL 720
Cdd:cd00588   79 VGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGssnaPGISGATILGDGRVVLILDVDKL 136
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 594-720 1.25e-19

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: 85.33  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  594 LMVGVAGHPFALPLASVNEIFHLD-LSRTNVVDGQL--TIIVRDKSIPLFYLQNWLAPKAgivELRKGHGHVVIVQLGSQ 670
Cdd:pfam01584   2 LLFRLGGETFAIPISKVREILRPPpITPIPGAPGYVlgVINLRGEVLPVIDLRRLLGLPP---TEPRERTRVVVVEVGGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515631512  671 RVGFVVDTLIGQEEVVIKPLDKLLQGTPG---MAGATITSDGHIALILDVPDL 720
Cdd:pfam01584  79 VVGLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 6-104 1.50e-18

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: 80.89  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512   6 DEDILQDFLVEAGEILELLSEQLVELENNpddkDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGqRSVT 85
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELEDA----EDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                         90
                 ....*....|....*....
gi 515631512  86 SGLMDTMLQALDTVNVQFR 104
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 8-97 3.95e-16

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: 74.21  E-value: 3.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512     8 DILQDFLVEAGEILELLSEQLVELENNPDDKDLlNAIFRGFHTVKGGAGFLALTELVDTCHGAENVFDILRNGQRSVTSG 87
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKALDAQDV-NEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|
gi 515631512    88 LMDTMLQALD 97
Cdd:smart00073  80 LLDLLLELVD 89
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 447-587 1.07e-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: 73.56  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512  447 ADPLIHLVRNSVDHGIEmpndrvAAGKSQTGKVILSasqEGDHIELAIVDDGGGMDPDKLRaiavkrglmdedaasrlsn 526
Cdd:pfam02518   3 ELRLRQVLSNLLDNALK------HAAKAGEITVTLS---EGGELTLTVEDNGIGIPPEDLP------------------- 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631512  527 kecfnLIFAPgFSSKEQISdISGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:pfam02518  55 -----RIFEP-FSTADKRG-GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
415-587 5.55e-14

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 73.79  E-value: 5.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 415 VVRDLARSL-----KKDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDHGiempndrvaagkSQTGKVILSA 483
Cdd:COG0642  187 LLEEVVELFrplaeEKGIELE-----LDLPDDLPTVRGDPdrlrqvLLNLLSNAIKYT------------PEGGTVTVSV 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 484 SQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnkecfnliFAPGFSSKEQISDiSGRGVGMDVVKTAINT 563
Cdd:COG0642  250 RREGDRVRISVEDTGPGIPPEDLERI------------------------FEPFFRTDPSRRG-GGTGLGLAIVKRIVEL 304

                        170       180
                 ....*....|....*....|....
gi 515631512 564 LNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG0642  305 HGGTIEVESEPGKGTTFTVTLPLA 328
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 414-587 3.65e-13

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 71.75  E-value: 3.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 414 RVVRDLARSL-----KKDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDhgiempndrvAAGKSQTGKVILS 482
Cdd:COG4191  219 ELIDEALELLrprlkARGIEVE-----LDLPPDLPPVLGDPgqleqvLLNLLINAID----------AMEEGEGGRITIS 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 483 ASQEGDHIELAIVDDGGGMDPDKLRAiavkrglmdedaasrlsnkecfnlIFAPGFSSKEQisdISGRGVGMDVVKTAIN 562
Cdd:COG4191  284 TRREGDYVVISVRDNGPGIPPEVLER------------------------IFEPFFTTKPV---GKGTGLGLSISYGIVE 336

                        170       180
                 ....*....|....*....|....*
gi 515631512 563 TLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG4191  337 KHGGRIEVESEPGGGTTFTITLPLA 361
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 342-400 6.02e-13

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: 64.18  E-value: 6.02e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515631512  342 TVRVDTSTLDTIMNMVGELVLVRNRLVSL-------GLNSNDEEMSKAVSNLDVVTADLQGAVMKT 400
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLlerleeyGGDTLLEELKEALQQLDRLTRELQEAVMKI 66
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 8-99 1.05e-12

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


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 63.91  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512    8 DILQDFLVEAGEILELLSEQLvelennpdDKDLLNAIFRGFHTVKGGAGFLALTELVDTCHGAENVfdiLRNGQRSVTSG 87
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDPE 69

                          90
                  ....*....|..
gi 515631512   88 LMDTMLQALDTV 99
Cdd:pfam01627  70 LLEALRDLLEAL 81
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
377-587 3.70e-12

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 66.85  E-value: 3.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 377 EEMSKAVSN-LDVvtADLQGAVMKTRMQPIkkvfgRFPRVVRDLARSLK-----KDIVLEMrgeetDLDKNLVEALADP- 449
Cdd:COG2205   64 ERLLRLIEDlLDL--SRLESGKLSLELEPV-----DLAELLEEAVEELRplaeeKGIRLEL-----DLPPELPLVYADPe 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 450 -----LIHLVRNSVDHGiempndrvaagkSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrl 524
Cdd:COG2205  132 lleqvLANLLDNAIKYS------------PPGGTITISARREGDGVRISVSDNGPGIPEEELERI--------------- 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515631512 525 snkecfnliFAPgFSSKEQISDISGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG2205  185 ---------FER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
416-587 5.14e-12

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 67.95  E-value: 5.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 416 VRDLARS-LKKDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDHgieMPNDrvaagksqtGKVILSASQE-- 486
Cdd:COG3852  213 VLELLRAeAPKNIRIV-----RDYDPSLPEVLGDPdqliqvLLNLVRNAAEA---MPEG---------GTITIRTRVErq 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 487 --------GDHIELAIVDDGGGMDPDklraiavkrgLMDEdaasrlsnkecfnlIFAPGFSSKEQisdisGRGVGMDVVK 558
Cdd:COG3852  276 vtlgglrpRLYVRIEVIDNGPGIPEE----------ILDR--------------IFEPFFTTKEK-----GTGLGLAIVQ 326

                        170       180
                 ....*....|....*....|....*....
gi 515631512 559 TAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG3852  327 KIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 400-587 1.18e-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: 67.29  E-value: 1.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 400 TRMQPIKKVFGRFPRVVRDLARSLK-----KDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDHGiempndr 468
Cdd:COG5000  266 ARLPEPQLEPVDLNELLREVLALYEpalkeKDIRLE-----LDLDPDLPEVLADRdqleqvLINLLKNAIEAI------- 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 469 vaagkSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrlsnkecfNLIFAPGFSSKEqisdiS 548
Cdd:COG5000  334 -----EEGGEIEVSTRREDGRVRIEVSDNGPGIPEEVL------------------------ERIFEPFFTTKP-----K 379

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515631512 549 GRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG5000  380 GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 419-589 1.33e-11

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 67.18  E-value: 1.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 419 LARSLKKDIVLEMRgEETDLDKNLVEALAdpLIHLVRNSVDHGIEMpndrVAAGKSQTGKVILSASQEGDHIELAIVDDG 498
Cdd:COG3290  254 AARARERGIDLTID-IDSDLPDLPLSDTD--LVTILGNLLDNAIEA----VEKLPEEERRVELSIRDDGDELVIEVEDSG 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 499 GGMDPDKLRAIavkrglmdedaasrlsnkecfnliFAPGFSSKEQisdiSGRGVGMDVVKTAINTLNGSIDIDSEMGQGT 578
Cdd:COG3290  327 PGIPEELLEKI------------------------FERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGT 378

                        170
                 ....*....|.
gi 515631512 579 KITIKVPLTLA 589
Cdd:COG3290  379 VFTVRLPKEGE 389
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 335-587 2.27e-10

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: 63.60  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 335 KKQQAEATVRVDTstldtiMNMVGELVL-----VRNRLVSL---------GLNSNDEEMSKAVSNLDVVTADLQGAVMKT 400
Cdd:COG5805  271 KKEAEELMARSEK------LSIAGQLAAgiaheIRNPLTSIkgflqllqpGIEDKEEYFDIMLSELDRIESIISEFLALA 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 401 RMQPIKKVFGRFPRVVRDL-----ARSLKKDIVLEMRGEETD----LDKNLVEALadpLIHLVRNSVDhgiEMPNDrvaa 471
Cdd:COG5805  345 KPQAVNKEKENINELIQDVvtlleTEAILHNIQIRLELLDEDpfiyCDENQIKQV---FINLIKNAIE---AMPNG---- 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 472 gksqtGKVILSASQEGDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrlsnkecfNLIFAPGFSSKEQisdisGRG 551
Cdd:COG5805  415 -----GTITIHTEEEDNSVIIRVIDEGIGIPEERL------------------------KKLGEPFFTTKEK-----GTG 460

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 515631512 552 VGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLT 587
Cdd:COG5805  461 LGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
453-587 3.07e-10

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 63.11  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 453 LVRNSVDHGIEmpndrvaaGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIAvkrglmdedaaSRLSNKEcfnl 532
Cdd:COG2972  344 LVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLL-----------EELSSKG---- 400

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515631512 533 ifapgfsskeqisdiSGRGVGMDVVKTAINTLNG---SIDIDSEMGQGTKITIKVPLT 587
Cdd:COG2972  401 ---------------EGRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLE 443
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 450-585 1.27e-09

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: 55.76  E-value: 1.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 450 LIHLVRNSVDHGIempnDRVAAGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRaiavkrglmdedaasrlsnkec 529
Cdd:cd16915    1 LITIVGNLIDNAL----DALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRD---------------------- 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515631512 530 fnLIFAPGFSSKEQisdiSGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVP 585
Cdd:cd16915   55 --KVFERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 453-585 1.32e-09

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


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 55.91  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 453 LVRNSVDHGIEmpndrvaaGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaASRLSNkecfnl 532
Cdd:cd16956    9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLARI-----------LIRSSN------ 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515631512 533 ifapgfsskeqisdisgrGVGMDVVKTAINTLNGS---IDIDSEMGQGTKITIKVP 585
Cdd:cd16956   64 ------------------GLGLNLVDKRLRQAFGNdygLDIECAPGEGTRITIRLP 101
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
379-586 1.63e-09

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 60.57  E-value: 1.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 379 MSKAVSNLDVVTADLQGAVMKTRMQP----IKKVFGRFPRVVRDLARSlkKDIVLEMRGEETdldknLVEALADP----- 449
Cdd:PRK10364 279 MAKEADRLNRVVSELLELVKPTHLALqavdLNDLINHSLQLVSQDANS--REIQLRFTANDT-----LPEIQADPdrltq 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 450 -LIHLVRNSVDhgiEMPndrvaagksQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnke 528
Cdd:PRK10364 352 vLLNLYLNAIQ---AIG---------QHGVISVTASESGAGVKISVTDSGKGIAADQLEAI------------------- 400

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515631512 529 cfnliFAPGFSSKEQisdisGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPL 586
Cdd:PRK10364 401 -----FTPYFTTKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 450-585 2.74e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 57.23  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 450 LIHLVRNSVDHGIEmpndrvAAGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnkec 529
Cdd:PRK11086 434 LITILGNLIENALE------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAI-------------------- 487

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515631512 530 fnliFAPGFSSKEqisdiSGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVP 585
Cdd:PRK11086 488 ----FDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 435-586 1.05e-07

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: 54.98  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 435 ETDLDKNLVEALADP------LIHLVRNsvdhGIE-MPNDrvaagksqtGKVILSAS-QEGDHIELAIVDDGGGMDPDKL 506
Cdd:COG5809  363 ELELEDDIPDILGDEnqlkqvFINLLKN----AIEaMPEG---------GNITIETKaEDDDKVVISVTDEGCGIPEERL 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 507 raiavKRglmdedaasrlsnkecfnlIFAPGFSSKEQisdisGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPL 586
Cdd:COG5809  430 -----KK-------------------LGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPI 480
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
414-586 1.27e-07

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 54.56  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 414 RVVRDL-ARSLKKDIVLEMrgeetDLDKNLVEALADP------LIHLVRNSVDHGiempndrvaagkSQTGKVILSASQE 486
Cdd:COG5002  248 EVVEELrPLAEEKGIELEL-----DLPEDPLLVLGDPdrleqvLTNLLDNAIKYT------------PEGGTITVSLREE 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 487 GDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrlsnkecfNLIFAPGF-SSKEQISDISGRGVGMDVVKTAINTLN 565
Cdd:COG5002  311 DDQVRISVRDTGIGIPEEDL------------------------PRIFERFYrVDKSRSRETGGTGLGLAIVKHIVEAHG 366

                        170       180
                 ....*....|....*....|.
gi 515631512 566 GSIDIDSEMGQGTKITIKVPL 586
Cdd:COG5002  367 GRIWVESEPGKGTTFTITLPL 387
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 414-587 1.00e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 51.83  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 414 RVVRDLARSL-KKDIVLEMRGEETDLDKNLVEALAdpLI-H-LVRNSVDHGiempndrvaAGKSQTGKVILSASQEGDHI 490
Cdd:COG3920  367 ELLEPLRDSYgGRGIRIELDGPDVELPADAAVPLG--LIlNeLVTNALKHA---------FLSGEGGRIRVSWRREDGRL 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 491 ELAIVDDGGGMDPDklraiavkrglmdedaasrlsnkecfnlifapgfsskeqISDISGRGVGMDVVKTAINTLNGSIDI 570
Cdd:COG3920  436 RLTVSDNGVGLPED---------------------------------------VDPPARKGLGLRLIRALVRQLGGTLEL 476

                        170
                 ....*....|....*..
gi 515631512 571 DSEmgQGTKITIKVPLT 587
Cdd:COG3920  477 DRP--EGTRVRITFPLA 491
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
435-586 1.46e-06

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 51.51  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 435 ETDLDKNLVEALADP------LIHLVRNSVDhgiempndrvaaGKSQTGKVILSASQEGD-HIELAIVDDGGGMDPDKLR 507
Cdd:PRK11360 484 ETELDNELPPIWADPellkqvLLNILINAVQ------------AISARGKIRIRTWQYSDgQVAVSIEDNGCGIDPELLK 551

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515631512 508 AIavkrglmdedaasrlsnkecfnliFAPGFSSKEQisdisGRGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPL 586
Cdd:PRK11360 552 KI------------------------FDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 474-585 2.25e-06

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: 46.90  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 474 SQTGKVILSASQEGDHIELAIVDDGGGMDPDKlraiaVKRglmdedaasrlsnkecfnlIFAPGFSSKEQISDISGRGVG 553
Cdd:cd16948   22 KQGGKIEIYSETNEQGVVLSIKDFGIGIPEED-----LPR-------------------VFDKGFTGENGRNFQESTGMG 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515631512 554 MDVVKTAINTLNGSIDIDSEMGQGTKITIKVP 585
Cdd:cd16948   78 LYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 470-586 2.06e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 43.95  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 470 AAGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnkecfnliFAPGFSSKEQISdisG 549
Cdd:cd16943   16 AQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRI------------------------FDPFFTTKPVGE---G 68

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515631512 550 RGVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPL 586
Cdd:cd16943   69 TGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 453-585 2.26e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340401 [Multi-domain]  Cd Length: 103  Bit Score: 43.97  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 453 LVRNSVDHGIEMpndrvaagKSQTGKVILSASQEGDHIELAIVDDGGGMDPDklraiavkrglmdedaasrlsnkecfnL 532
Cdd:cd16924    9 LVENAIQHGLSP--------LTDKGVVTISALKEDNHVMIEVEDNGRGIDPK---------------------------V 53

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515631512 533 IFAPGFSSKEqisdisGRGVGMDVVKTAINTLNG---SIDIDSEMGQGTKITIKVP 585
Cdd:cd16924   54 LNILGKKPKE------GNGIGLYNVHQRLILLFGedyGIHIASEPDKGTRITFTIP 103
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 486-585 3.13e-05

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: 43.91  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 486 EGDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnkecfnliFAPGFSSKEQISdisGRGVGMDVVKTAINTLN 565
Cdd:cd16919   44 PGNYVCLEVSDTGSGMPAEVLRRA------------------------FEPFFTTKEVGK---GTGLGLSMVYGFVKQSG 96

                         90       100
                 ....*....|....*....|
gi 515631512 566 GSIDIDSEMGQGTKITIKVP 585
Cdd:cd16919   97 GHLRIYSEPGVGTTVRIYLP 116
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 477-586 3.30e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 43.47  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 477 GKVILSASQEGDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrlsnkecfNLIFAPGFSSKEQISDIS-GRGVGMD 555
Cdd:cd16949   18 SKILLDISQDGDQWTITITDDGPGVPEDQL------------------------EQIFLPFYRVDSARDRESgGTGLGLA 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 515631512 556 VVKTAINTLNGSIDIDSEMGQGTKITIKVPL 586
Cdd:cd16949   74 IAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
PRK15347 PRK15347
two component system sensor kinase;
474-605 8.14e-04

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 42.71  E-value: 8.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 474 SQTGKVILSASQEGDHIELAIVDDGGGMDPDKLraiavkrglmdedaasrlsnkecfNLIFAPGFsskeQISD-ISGRGV 552
Cdd:PRK15347 529 TETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQ------------------------QQIFTPFY----QADThSQGTGL 580

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515631512 553 GMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLTLAILPTLMVGVAGHPFAL 605
Cdd:PRK15347 581 GLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKGELSAPLAL 633
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 422-504 1.01e-03

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: 39.71  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 422 SLKKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEmpnDRvaagksQTGKVILSASQEGDHIELAIVDDGGGM 501
Cdd:cd16951   16 HAVGDIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAFS---DR------EGGTITIRSVVDGDYLRITVIDDGVGL 86


                 ...
gi 515631512 502 DPD 504
Cdd:cd16951   87 PQD 89
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
487-587 1.46e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 41.97  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 487 GDHIELAIVDDGGGMDPDKLRAIavkrglmdedaasrlsnkecfnliFAPGFSSKEQisdisGRGVGMDVVKTAINTLNG 566
Cdd:PRK13837 605 GRYVLLRVSDTGAGIDEAVLPHI------------------------FEPFFTTRAG-----GTGLGLATVHGIVSAHAG 655

                         90       100
                 ....*....|....*....|.
gi 515631512 567 SIDIDSEMGQGTKITIKVPLT 587
Cdd:PRK13837 656 YIDVQSTVGRGTRFDVYLPPS 676
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
453-507 4.94e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 37.59  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515631512 453 LVRNSVDHGiempndrvaAGKSQTGKVILSASQEGDHIELAIVDDGGGMDPDKLR 507
Cdd:COG2172   42 AVTNAVRHA---------YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLP 87
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
476-595 5.42e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 40.34  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 476 TGKVILSASQEGDHIELAIVDDGGGMDPdklraiavkrglmdedaasrlsnKECFNLiFAPGFsskeQI-----SDISGR 550
Cdd:PRK10841 580 TGCIVLHVRVDGDYLSFRVRDTGVGIPA-----------------------KEVVRL-FDPFF----QVgtgvqRNFQGT 631

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515631512 551 GVGMDVVKTAINTLNGSIDIDSEMGQGTKITIKVPLTLAILPTLM 595
Cdd:PRK10841 632 GLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKK 676
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
594-721 6.95e-03

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 37.93  E-value: 6.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631512 594 LMVGVAGHPFALPLASVNEIFHL-DLSR----TNVVDGqlTIIVRDKSIPLFYLQNWLAPKAGIVELRKghgHVVIVQLG 668
Cdd:COG0835   11 LTFRLGGERYAIPIEKVREILPLpPITPvpgaPPWVLG--VINLRGRVVPVIDLRALLGLPPTEDTERT---RIIVLEVG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515631512 669 SQRVGFVVDTLIGQEEV---VIKPLDKLL-QGTPGMAGATITSDGHIALILDVPDLL 721
Cdd:COG0835   86 GRVVGLLVDSVSGVVRIdpdDIEPPPELLsGGLAPFITGVAKLDDRLILLLDLEKLL 142
Rib_recp_KP_reg pfam05104
Ribosome receptor lysine/proline rich region; This highly conserved region is found towards ...
 108-164 7.13e-03

Ribosome receptor lysine/proline rich region; This highly conserved region is found towards the C-terminus of the transmembrane domain. The function is unclear.


Pssm-ID: 461548 [Multi-domain]  Cd Length: 140  Bit Score: 37.41  E-value: 7.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515631512  108 DQEPLVPADQSLLDELHRLCKPESADEVAPVEAPAPIIPEPVVAAPEPVIAPEPTAE 164
Cdd:pfam05104  52 ESEQADESEEEPREFKTPDEAPSAALEPEPVPTPVPAPVEPEPAPPSESPAPSPKEK 108
 
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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