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Conserved domains on  [gi|491522875|ref|WP_005380503|]
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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];
6-745 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 671.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   6 DEDILQDFLIEAGEILELLSEQLVELENNPEDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  86 QNLMDTMLKALDTVNTQFQAVQDREPLEAADPELLEELhrlckPESEDEVAATVVEEpvatpepiipepiieepaapsap 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARL-----DASEEAIEEVVADE----------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 166 ssvgsvdeitqdefeklldelhgkgsapgtsmsatpttpseppqssapsvesgditddeferlldelhgvgkspstaeaa 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 246 asasVPVEPPkaaepsapvssssnqdsdlmtdeefeklldelhgsgkgptleeldmatkpASANVEQSPAKPEPvakpap 325
Cdd:COG0643  135 ----VEISPP--------------------------------------------------APAALEPAPAAAPP------ 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 326 vqaapapkpeskpvavKEEAKAPAVKKPQAEATVRVDTSTLDTIMNMVGELVLVRNRLLSLGLNSDNE---EMSKAVANL 402
Cdd:COG0643  155 ----------------AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQL 218

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 403 DVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPD 482
Cdd:COG0643  219 SRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPE 298

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 483 ARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAAARLTDKECFNLIFAPGFSSKDKISD 562
Cdd:COG0643  299 ERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTD 378

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 563 ISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGVGGHPFALPLASVSEIFHLDLSRTNVVDG 642
Cdd:COG0643  379 LSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEG 458

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 643 QLTIIVREKSIPLFYLQNWLASKSQnvQERTGHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPLDNLLQGTPGMAGATIT 722
Cdd:COG0643  459 REVIRLRGELLPLVRLGELLGLPGA--EPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATIL 536

                        730       740
                 ....*....|....*....|...
gi 491522875 723 SDGHIALILDVPDLLKRYAAASR 745
Cdd:COG0643  537 GDGRVALILDVAALVRSARARAR 559
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-745 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 671.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   6 DEDILQDFLIEAGEILELLSEQLVELENNPEDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  86 QNLMDTMLKALDTVNTQFQAVQDREPLEAADPELLEELhrlckPESEDEVAATVVEEpvatpepiipepiieepaapsap 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARL-----DASEEAIEEVVADE----------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 166 ssvgsvdeitqdefeklldelhgkgsapgtsmsatpttpseppqssapsvesgditddeferlldelhgvgkspstaeaa 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 246 asasVPVEPPkaaepsapvssssnqdsdlmtdeefeklldelhgsgkgptleeldmatkpASANVEQSPAKPEPvakpap 325
Cdd:COG0643  135 ----VEISPP--------------------------------------------------APAALEPAPAAAPP------ 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 326 vqaapapkpeskpvavKEEAKAPAVKKPQAEATVRVDTSTLDTIMNMVGELVLVRNRLLSLGLNSDNE---EMSKAVANL 402
Cdd:COG0643  155 ----------------AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQL 218

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 403 DVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPD 482
Cdd:COG0643  219 SRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPE 298

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 483 ARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAAARLTDKECFNLIFAPGFSSKDKISD 562
Cdd:COG0643  299 ERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTD 378

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 563 ISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGVGGHPFALPLASVSEIFHLDLSRTNVVDG 642
Cdd:COG0643  379 LSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEG 458

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 643 QLTIIVREKSIPLFYLQNWLASKSQnvQERTGHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPLDNLLQGTPGMAGATIT 722
Cdd:COG0643  459 REVIRLRGELLPLVRLGELLGLPGA--EPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATIL 536

                        730       740
                 ....*....|....*....|...
gi 491522875 723 SDGHIALILDVPDLLKRYAAASR 745
Cdd:COG0643  537 GDGRVALILDVAALVRSARARAR 559
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-736 7.48e-114

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 359.04  E-value: 7.48e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   8 DILQDFLIEAGEILELLSEQLVELENNPEDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVTQN 87
Cdd:PRK10547   5 DFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  88 LMDTMLKALDTVNTQFQAVQD-REPLEAADPELLEELHRLCKpESEDEVAATVVEEPVATPEPIIPEPIieepaapSAPS 166
Cdd:PRK10547  85 IINLFLETKDIMQEQLDAYKTsQEPDAASFEYICQALRQLAL-EAKGETPSAVTRLSVVAIQEKSEPQD-------ESPR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 167 SVG----SVDEITQDEFEKLLDELHGKGsapgtsmsatptTPSEPPQSSApSVES---GDITDDEFERLLdelhgvgksp 239
Cdd:PRK10547 157 SQSglriILSRLKAGEVDLLEEELGNLG------------TLTDVVKGAD-SLEAtlpGSVAEDDITAVL---------- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 240 staeaaasaSVPVEPPKAAEPSAPVSSssnqdsdlmtdeefeklldelhgsgkgPTLEELDMATKPASANVEQSPAKPEP 319
Cdd:PRK10547 214 ---------CFVIEADQITFETAVAAP---------------------------QEKAEETTEVVEVSPKISVPPVLKLA 257

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 320 VakpapvqaapapkpeSKPVAVKEEAKAPAvkKPQAEATVRVDTSTLDTIMNMVGELVLVRNRLL--SLGLN-SDNEEMS 396
Cdd:PRK10547 258 A---------------EQAPAGRVEREKTA--RSSESTSIRVAVEKVDQLINLVGELVITQSMLAqrSSELDpVNHGDLI 320

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 397 KAVANLDVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDH 476
Cdd:PRK10547 321 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 477 GIEMPDARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAaarLTDKECFNLIFAPGFSS 556
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFST 477

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 557 KDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGVGGHPFALPLASVSEIFH---LD 633
Cdd:PRK10547 478 AEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQpreED 557

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 634 LSrtNVVDGQLTIIVREKSIPLFYLqnWLASKSQNVQERTGHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPLDNLLQGT 713
Cdd:PRK10547 558 LH--PLAGGERVLEVRGEYLPLVEL--WKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKV 633

                        730       740
                 ....*....|....*....|...
gi 491522875 714 PGMAGATITSDGHIALILDVPDL 736
Cdd:PRK10547 634 PGISAATILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 424-601 6.40e-87

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: 271.38  E-value: 6.40e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 424 VFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPDARAKAGKSRTGKVILSASQEG 503
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 504 DHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAAARLTDKECFNLIFAPGFSSKDKISDISGRGVGMDVVKTAINTLNGS 583
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 491522875 584 IDIDSELGKGTKITIKVP 601
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
597-737 2.21e-24

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 99.24  E-value: 2.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   597 TIKVPLTLAILPTLMvgvgghpFALPLASVSEIFHLD-LSR--TNVVDGQLTIIVREKSIPLFYLQNWLaskSQNVQERT 673
Cdd:smart00260   1 TIRLPLTFAIGKDET-------YAIPIAAVREILRPPpITPipGAPGYVLGVINLRGEVLPVVDLRRLL---GLPPEPPT 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875   674 GHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPL----DNLLQGTPGMAGATITSDGHIALILDVPDLL 737
Cdd:smart00260  71 DETRVIVVETGDRKVGLVVDSVLGVREVVVKSIepppPVSLSNAPGISGATILGDGRVVLILDVDKLL 138
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 610-736 3.94e-22

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: 92.65  E-value: 3.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  610 LMVGVGGHPFALPLASVSEIFHLD-LSRTNVVDGQL--TIIVREKSIPLFYLQNWLASKSQNVQERTghgHVVIVQIGNQ 686
Cdd:pfam01584   2 LLFRLGGETFAIPISKVREILRPPpITPIPGAPGYVlgVINLRGEVLPVIDLRRLLGLPPTEPRERT---RVVVVEVGGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491522875  687 RVGFVVDTLIGQEEVVIKPLDNLLQGTPG---MAGATITSDGHIALILDVPDL 736
Cdd:pfam01584  79 VVGLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
6-745 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 671.12  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   6 DEDILQDFLIEAGEILELLSEQLVELENNPEDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVT 85
Cdd:COG0643    3 MDELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  86 QNLMDTMLKALDTVNTQFQAVQDREPLEAADPELLEELhrlckPESEDEVAATVVEEpvatpepiipepiieepaapsap 165
Cdd:COG0643   83 PELIDLLLEALDALRALLDALEAGGEPPADISALLARL-----DASEEAIEEVVADE----------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 166 ssvgsvdeitqdefeklldelhgkgsapgtsmsatpttpseppqssapsvesgditddeferlldelhgvgkspstaeaa 245
Cdd:COG0643      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 246 asasVPVEPPkaaepsapvssssnqdsdlmtdeefeklldelhgsgkgptleeldmatkpASANVEQSPAKPEPvakpap 325
Cdd:COG0643  135 ----VEISPP--------------------------------------------------APAALEPAPAAAPP------ 154

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 326 vqaapapkpeskpvavKEEAKAPAVKKPQAEATVRVDTSTLDTIMNMVGELVLVRNRLLSLGLNSDNE---EMSKAVANL 402
Cdd:COG0643  155 ----------------AEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAEELEDEslrELEEALEQL 218

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 403 DVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPD 482
Cdd:COG0643  219 SRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPE 298

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 483 ARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAAARLTDKECFNLIFAPGFSSKDKISD 562
Cdd:COG0643  299 ERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFAPGFSTAEEVTD 378

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 563 ISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGVGGHPFALPLASVSEIFHLDLSRTNVVDG 642
Cdd:COG0643  379 LSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRLDPDDIETVEG 458

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 643 QLTIIVREKSIPLFYLQNWLASKSQnvQERTGHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPLDNLLQGTPGMAGATIT 722
Cdd:COG0643  459 REVIRLRGELLPLVRLGELLGLPGA--EPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATIL 536

                        730       740
                 ....*....|....*....|...
gi 491522875 723 SDGHIALILDVPDLLKRYAAASR 745
Cdd:COG0643  537 GDGRVALILDVAALVRSARARAR 559
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 8-736 7.48e-114

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 359.04  E-value: 7.48e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   8 DILQDFLIEAGEILELLSEQLVELENNPEDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVTQN 87
Cdd:PRK10547   5 DFYQTFFDEADELLADMEQHLLVLDPEAPDAEQLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  88 LMDTMLKALDTVNTQFQAVQD-REPLEAADPELLEELHRLCKpESEDEVAATVVEEPVATPEPIIPEPIieepaapSAPS 166
Cdd:PRK10547  85 IINLFLETKDIMQEQLDAYKTsQEPDAASFEYICQALRQLAL-EAKGETPSAVTRLSVVAIQEKSEPQD-------ESPR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 167 SVG----SVDEITQDEFEKLLDELHGKGsapgtsmsatptTPSEPPQSSApSVES---GDITDDEFERLLdelhgvgksp 239
Cdd:PRK10547 157 SQSglriILSRLKAGEVDLLEEELGNLG------------TLTDVVKGAD-SLEAtlpGSVAEDDITAVL---------- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 240 staeaaasaSVPVEPPKAAEPSAPVSSssnqdsdlmtdeefeklldelhgsgkgPTLEELDMATKPASANVEQSPAKPEP 319
Cdd:PRK10547 214 ---------CFVIEADQITFETAVAAP---------------------------QEKAEETTEVVEVSPKISVPPVLKLA 257

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 320 VakpapvqaapapkpeSKPVAVKEEAKAPAvkKPQAEATVRVDTSTLDTIMNMVGELVLVRNRLL--SLGLN-SDNEEMS 396
Cdd:PRK10547 258 A---------------EQAPAGRVEREKTA--RSSESTSIRVAVEKVDQLINLVGELVITQSMLAqrSSELDpVNHGDLI 320

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 397 KAVANLDVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDH 476
Cdd:PRK10547 321 TSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRNSLDH 400

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 477 GIEMPDARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAaarLTDKECFNLIFAPGFSS 556
Cdd:PRK10547 401 GIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLAVSEN---MSDEEVGMLIFAPGFST 477

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 557 KDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGVGGHPFALPLASVSEIFH---LD 633
Cdd:PRK10547 478 AEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRVADEVFILPLNAVMESLQpreED 557

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 634 LSrtNVVDGQLTIIVREKSIPLFYLqnWLASKSQNVQERTGHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPLDNLLQGT 713
Cdd:PRK10547 558 LH--PLAGGERVLEVRGEYLPLVEL--WKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNYRKV 633

                        730       740
                 ....*....|....*....|...
gi 491522875 714 PGMAGATITSDGHIALILDVPDL 736
Cdd:PRK10547 634 PGISAATILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 424-601 6.40e-87

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: 271.38  E-value: 6.40e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 424 VFGRFPRVVRDLARNLNKDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIEMPDARAKAGKSRTGKVILSASQEG 503
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 504 DHIELSIVDDGGGMDPNKLRGIAVKRGMMDEDAAARLTDKECFNLIFAPGFSSKDKISDISGRGVGMDVVKTAINTLNGS 583
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 491522875 584 IDIDSELGKGTKITIKVP 601
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 604-736 2.27e-38

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: 138.85  E-value: 2.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 604 LAILPTLMVGVGGHPFALPLASVSEIFHLDLSRTNVVDG-QLTIIVREKSIPLFYLQNWLasKSQNVQERTGHGHVVIVQ 682
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGgKEVINVRGELLPLVRLGELF--NVRGENEEPDEGVVVVVR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491522875 683 IGNQRVGFVVDTLIGQEEVVIKPLDNLLQGTPGMAGATITSDGHIALILDVPDL 736
Cdd:cd00731   79 TGGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
597-737 2.21e-24

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 99.24  E-value: 2.21e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   597 TIKVPLTLAILPTLMvgvgghpFALPLASVSEIFHLD-LSR--TNVVDGQLTIIVREKSIPLFYLQNWLaskSQNVQERT 673
Cdd:smart00260   1 TIRLPLTFAIGKDET-------YAIPIAAVREILRPPpITPipGAPGYVLGVINLRGEVLPVVDLRRLL---GLPPEPPT 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875   674 GHGHVVIVQIGNQRVGFVVDTLIGQEEVVIKPL----DNLLQGTPGMAGATITSDGHIALILDVPDLL 737
Cdd:smart00260  71 DETRVIVVETGDRKVGLVVDSVLGVREVVVKSIepppPVSLSNAPGISGATILGDGRVVLILDVDKLL 138
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 461-603 3.30e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 95.02  E-value: 3.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   461 ALADPLIHLVRNSVDHGIempdaraKAGKSRtGKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaarl 540
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAI-------KYTPEG-GRITVTLERDGDHVEITVEDNGPGIPPEDL------------------ 54

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491522875   541 tdkecfNLIFAPGFSSKDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:smart00387  55 ------EKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 610-736 3.94e-22

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: 92.65  E-value: 3.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  610 LMVGVGGHPFALPLASVSEIFHLD-LSRTNVVDGQL--TIIVREKSIPLFYLQNWLASKSQNVQERTghgHVVIVQIGNQ 686
Cdd:pfam01584   2 LLFRLGGETFAIPISKVREILRPPpITPIPGAPGYVlgVINLRGEVLPVIDLRRLLGLPPTEPRERT---RVVVVEVGGQ 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491522875  687 RVGFVVDTLIGQEEVVIKPLDNLLQGTPG---MAGATITSDGHIALILDVPDL 736
Cdd:pfam01584  79 VVGLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 606-736 4.04e-21

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: 90.03  E-value: 4.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 606 ILPTLMVGVGGHPFALPLASVSEIFHLDLSR---TNVVDGQLTIIVREKSIPLFYLQNWLASKSQNVqeRTGHGHVVIVQ 682
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITrvpNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEP--DTDETRIVVVE 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875 683 IGNQRVGFVVDTLIGQEEVVIKPLDNLLQGT----PGMAGATITSDGHIALILDVPDL 736
Cdd:cd00588   79 VGDRKVGLVVDSVLGVLEVVIKDIEPPPDVGssnaPGISGATILGDGRVVLILDVDKL 136
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 6-104 4.33e-19

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: 82.43  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875   6 DEDILQDFLIEAGEILELLSEQLVELENNpedkDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGqRTVT 85
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELEDA----EDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVT 75

                         90
                 ....*....|....*....
gi 491522875  86 QNLMDTMLKALDTVNTQFQ 104
Cdd:cd00088   76 PELIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 8-97 6.30e-17

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: 76.52  E-value: 6.30e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875     8 DILQDFLIEAGEILELLSEQLVELENNPEDKDLlNAIFRGFHTVKGGAGFLSLAELVDTCHGAENVFDVLRNGQRTVTQN 87
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKALDAQDV-NEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|
gi 491522875    88 LMDTMLKALD 97
Cdd:smart00073  80 LLDLLLELVD 89
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 463-603 1.59e-16

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: 75.87  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875  463 ADPLIHLVRNSVDHGIempDARAKAGKsrtGKVILSasqEGDHIELSIVDDGGGMDPNKLRgiavkrgmmdedaaarltd 542
Cdd:pfam02518   3 ELRLRQVLSNLLDNAL---KHAAKAGE---ITVTLS---EGGELTLTVEDNGIGIPPEDLP------------------- 54

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491522875  543 kecfnLIFAPgFSSKDKISdISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:pfam02518  55 -----RIFEP-FSTADKRG-GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
451-603 2.29e-13

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 71.86  E-value: 2.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 451 ETDLDKNLVEALADP------LIHLVRNSVDHGiempdaraKAGksrtGKVILSASQEGDHIELSIVDDGGGMDPNKLRg 524
Cdd:COG0642  207 ELDLPDDLPTVRGDPdrlrqvLLNLLSNAIKYT--------PEG----GTVTVSVRREGDRVRISVEDTGPGIPPEDLE- 273

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491522875 525 iavkrgmmdedaaarltdkecfnLIFAPGFSSKDKISDiSGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:COG0642  274 -----------------------RIFEPFFRTDPSRRG-GGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
366-603 3.07e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.94  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 366 LDTIMNMVGELVLVRNRLLSLgLNSDNEEMSKAVAN-LDVVTADLQGAVMKTRMQPIKKVFGRFPRVVRDLARNLNKDIV 444
Cdd:COG2205   38 AELLLDEEDLSPEERRELLEI-IRESAERLLRLIEDlLDLSRLESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 445 LemrgeetDLDKNLVEALADP------LIHLVRNSVDHGiempdarakagkSRTGKVILSASQEGDHIELSIVDDGGGMD 518
Cdd:COG2205  117 L-------DLPPELPLVYADPelleqvLANLLDNAIKYS------------PPGGTITISARREGDGVRISVSDNGPGIP 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 519 PNKLrgiavkrgmmdedaaarltdkecfNLIFAPgFSSKDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITI 598
Cdd:COG2205  178 EEEL------------------------ERIFER-FYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232


                 ....*
gi 491522875 599 KVPLT 603
Cdd:COG2205  233 TLPLA 237
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 451-603 3.14e-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: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 451 ETDLDKNLVEALADP------LIHLVRNSVDhgiEMPDARAkagksrtGKVILSASQEGDHIELSIVDDGGGMDPnklrg 524
Cdd:COG4191  240 ELDLPPDLPPVLGDPgqleqvLLNLLINAID---AMEEGEG-------GRITISTRREGDYVVISVRDNGPGIPP----- 304

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491522875 525 iavkrgmmdeDAAARltdkecfnlIFAPGFSSKdkiSDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:COG4191  305 ----------EVLER---------IFEPFFTTK---PVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 358-416 5.48e-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: 5.48e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875  358 TVRVDTSTLDTIMNMVGELVLVRNRLLSL-------GLNSDNEEMSKAVANLDVVTADLQGAVMKT 416
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLlerleeyGGDTLLEELKEALQQLDRLTRELQEAVMKI 66
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 8-99 2.04e-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: 63.14  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875    8 DILQDFLIEAGEILELLSEQLvelennpeDKDLLNAIFRGFHTVKGGAGFLSLAELVDTCHGAEnvfDVLRNGQRTVTQN 87
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELE---DLLREGELPLDPE 69

                          90
                  ....*....|..
gi 491522875   88 LMDTMLKALDTV 99
Cdd:pfam01627  70 LLEALRDLLEAL 81
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
432-603 2.16e-12

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 69.10  E-value: 2.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 432 VRDLARN-LNKDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDHgieMPDarakagksrTGKVILSASQE-- 502
Cdd:COG3852  213 VLELLRAeAPKNIRIV-----RDYDPSLPEVLGDPdqliqvLLNLVRNAAEA---MPE---------GGTITIRTRVErq 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 503 --------GDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaarltDKecfnlIFAPGFSSKDKisdisGRGVGMDVVK 574
Cdd:COG3852  276 vtlgglrpRLYVRIEVIDNGPGIPEEIL-------------------DR-----IFEPFFTTKEK-----GTGLGLAIVQ 326

                        170       180
                 ....*....|....*....|....*....
gi 491522875 575 TAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:COG3852  327 KIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 416-603 2.95e-12

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: 69.22  E-value: 2.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 416 TRMQPIKKVFGRFPRVVRDLA-----RNLNKDIVLEmrgeeTDLDKNLVEALADP------LIHLVRNSVDHgieMPDAr 484
Cdd:COG5000  266 ARLPEPQLEPVDLNELLREVLalyepALKEKDIRLE-----LDLDPDLPEVLADRdqleqvLINLLKNAIEA---IEEG- 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 485 akagksrtGKVILSASQEGDHIELSIVDDGGGMDPnklrgiavkrgmmdeDAAARltdkecfnlIFAPGFSSKDKisdis 564
Cdd:COG5000  337 --------GEIEVSTRREDGRVRIEVSDNGPGIPE---------------EVLER---------IFEPFFTTKPK----- 379

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 491522875 565 GRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:COG5000  380 GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 435-605 4.18e-12

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 68.72  E-value: 4.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 435 LARNLNKDIVLEmrgEETDLDKNLVEALAdpLIHLVRNSVDHGIEmpdArAKAGKSRTGKVILSASQEGDHIELSIVDDG 514
Cdd:COG3290  256 RARERGIDLTID---IDSDLPDLPLSDTD--LVTILGNLLDNAIE---A-VEKLPEEERRVELSIRDDGDELVIEVEDSG 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 515 GGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPGFSSKDKisdiSGRGVGMDVVKTAINTLNGSIDIDSELGKGT 594
Cdd:COG3290  327 PGIPEELL------------------------EKIFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGT 378

                        170
                 ....*....|.
gi 491522875 595 KITIKVPLTLA 605
Cdd:COG3290  379 VFTVRLPKEGE 389
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 436-603 1.22e-11

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: 67.83  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 436 ARNLNKDIVLEMRGE--ETDLDKNLVEALadpLIHLVRNSVDhgiEMPDArakagksrtGKVILSASQEGDHIELSIVDD 513
Cdd:COG5805  371 AILHNIQIRLELLDEdpFIYCDENQIKQV---FINLIKNAIE---AMPNG---------GTITIHTEEEDNSVIIRVIDE 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 514 GGGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPGFSSKDKisdisGRGVGMDVVKTAINTLNGSIDIDSELGKG 593
Cdd:COG5805  436 GIGIPEERL------------------------KKLGEPFFTTKEK-----GTGLGLMVSYKIIENHNGTIDIDSKVGKG 486

                        170
                 ....*....|
gi 491522875 594 TKITIKVPLT 603
Cdd:COG5805  487 TTFTITLPLS 496
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
469-603 8.82e-11

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 64.65  E-value: 8.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 469 LVRNSVDHGIEmpdarakaGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIAvkrgmmdedaaarltdkecfnl 548
Cdd:COG2972  344 LVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLL---------------------- 393

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875 549 ifaPGFSSKDKisdisGRGVGMDVVKTAINTLNG---SIDIDSELGKGTKITIKVPLT 603
Cdd:COG2972  394 ---EELSSKGE-----GRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLE 443
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
366-602 1.43e-09

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 60.72  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 366 LDTIMNMVGELVLVRNRLLSLgLNSDNEEMSKAVANLDVVtADLQGAVMKTRMQPIkkvfgRFPRVVRDLARNL-----N 440
Cdd:COG5002  187 LELLLDGAADDPEERREYLEI-ILEEAERLSRLVNDLLDL-SRLESGELKLEKEPV-----DLAELLEEVVEELrplaeE 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 441 KDIVLEMrgeetDLDKNLVEALADP------LIHLVRNSVDHGiempdaraKAGksrtGKVILSASQEGDHIELSIVDDG 514
Cdd:COG5002  260 KGIELEL-----DLPEDPLLVLGDPdrleqvLTNLLDNAIKYT--------PEG----GTITVSLREEDDQVRISVRDTG 322

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 515 GGMDPNKLrgiavkrgmmdedaaARLTDKecfnlifapgF--SSKDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGK 592
Cdd:COG5002  323 IGIPEEDL---------------PRIFER----------FyrVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGK 377

                        250
                 ....*....|
gi 491522875 593 GTKITIKVPL 602
Cdd:COG5002  378 GTTFTITLPL 387
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 440-602 9.62e-09

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: 58.45  E-value: 9.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 440 NKDIVLEMRGEETDL--DKNLVEALadpLIHLVRNsvdhGIE-MPDArakagksrtGKVILSAS-QEGDHIELSIVDDGG 515
Cdd:COG5809  359 NVQIELELEDDIPDIlgDENQLKQV---FINLLKN----AIEaMPEG---------GNITIETKaEDDDKVVISVTDEGC 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 516 GMDPNKLrgiavKRgmmdedaaarltdkecfnlIFAPGFSSKDKisdisGRGVGMDVVKTAINTLNGSIDIDSELGKGTK 595
Cdd:COG5809  423 GIPEERL-----KK-------------------LGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKITVESEVGKGTT 473


                 ....*..
gi 491522875 596 ITIKVPL 602
Cdd:COG5809  474 FSITLPI 480
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 469-601 2.10e-08

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: 52.44  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 469 LVRNSVDHGIEmpdarakaGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRgiavkrgmmdedaaarltdkecfnl 548
Cdd:cd16956    9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMDPDTLA------------------------- 55

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875 549 ifapgfsskdKISDISGRGVGMDVVKTAINTLNGS---IDIDSELGKGTKITIKVP 601
Cdd:cd16956   56 ----------RILIRSSNGLGLNLVDKRLRQAFGNdygLDIECAPGEGTRITIRLP 101
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 505-601 5.40e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.07  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 505 HIELSivDDGGGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPGFSSKDKisdisGRGVGMDVVKTAINTLNGSI 584
Cdd:PRK11086 469 HCEVS--DDGPGIAPDEI------------------------DAIFDKGYSTKGS-----NRGVGLYLVKQSVENLGGSI 517

                         90
                 ....*....|....*..
gi 491522875 585 DIDSELGKGTKITIKVP 601
Cdd:PRK11086 518 AVESEPGVGTQFFVQIP 534
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 431-603 6.77e-08

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 55.68  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 431 VVRDLARNL-----NKDIVLEMRGEETDLDKNLVEALAdpLI-H-LVRNSVDHGiempdarakAGKSRTGKVILSASQEG 503
Cdd:COG3920  364 YLRELLEPLrdsygGRGIRIELDGPDVELPADAAVPLG--LIlNeLVTNALKHA---------FLSGEGGRIRVSWRRED 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 504 DHIELSIVDDGGGMDPNklrgiavkrgmmdedaaarltdkecfnlifapgfsskdkISDISGRGVGMDVVKTAINTLNGS 583
Cdd:COG3920  433 GRLRLTVSDNGVGLPED---------------------------------------VDPPARKGLGLRLIRALVRQLGGT 473

                        170       180
                 ....*....|....*....|
gi 491522875 584 IDIDSElgKGTKITIKVPLT 603
Cdd:COG3920  474 LELDRP--EGTRVRITFPLA 491
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 466-601 8.49e-08

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: 50.75  E-value: 8.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 466 LIHLVRNSVDHGIempDARAKAGKSrTGKVILSASQEGDHIELSIVDDGGGMDPNKLRgiavkrgmmdedaaarltdkec 545
Cdd:cd16915    1 LITIVGNLIDNAL---DALAATGAP-NKQVEVFLRDEGDDLVIEVRDTGPGIAPELRD---------------------- 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875 546 fnLIFAPGFSSKDKisdiSGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVP 601
Cdd:cd16915   55 --KVFERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
451-602 5.84e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 53.05  E-value: 5.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 451 ETDLDKNLVEALADP------LIHLVRNSVDhgiempdarakaGKSRTGKVILSASQEGD-HIELSIVDDGGGMDPNKLR 523
Cdd:PRK11360 484 ETELDNELPPIWADPellkqvLLNILINAVQ------------AISARGKIRIRTWQYSDgQVAVSIEDNGCGIDPELLK 551

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491522875 524 GIavkrgmmdedaaarltdkecfnliFAPGFSSKDKisdisGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPL 602
Cdd:PRK11360 552 KI------------------------FDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
395-602 6.07e-07

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 52.48  E-value: 6.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 395 MSKAVANLDVVTADLQGAVMKTRMQP----IKKVFGRFPRVVRDLARNlnKDIVLEMRGEETdldknLVEALADP----- 465
Cdd:PRK10364 279 MAKEADRLNRVVSELLELVKPTHLALqavdLNDLINHSLQLVSQDANS--REIQLRFTANDT-----LPEIQADPdrltq 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 466 -LIHLVRNSVDhgiEMPdarakagksRTGKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdeDAaarltdke 544
Cdd:PRK10364 352 vLLNLYLNAIQ---AIG---------QHGVISVTASESGAGVKISVTDSGKGIAADQL------------EA-------- 399

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875 545 cfnlIFAPGFSSKDKisdisGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPL 602
Cdd:PRK10364 400 ----IFTPYFTTKAE-----GTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 485-602 9.65e-07

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: 47.80  E-value: 9.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 485 AKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKLRGIavkrgmmdedaaarltdkecfnliFAPGFSSKdkiSDIS 564
Cdd:cd16943   15 AAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRI------------------------FDPFFTTK---PVGE 67

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 491522875 565 GRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPL 602
Cdd:cd16943   68 GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 493-601 9.79e-07

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: 48.05  E-value: 9.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 493 GKVILSASQEGDHIELSIVDDGGGMDPNKlrgiaVKRgmmdedaaarltdkecfnlIFAPGFSSKDKISDISGRGVGMDV 572
Cdd:cd16948   25 GKIEIYSETNEQGVVLSIKDFGIGIPEED-----LPR-------------------VFDKGFTGENGRNFQESTGMGLYL 80

                         90       100
                 ....*....|....*....|....*....
gi 491522875 573 VKTAINTLNGSIDIDSELGKGTKITIKVP 601
Cdd:cd16948   81 VKKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 469-601 4.42e-06

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: 45.90  E-value: 4.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 469 LVRNSVDHGIEMpdarakagKSRTGKVILSASQEGDHIELSIVDDGGGMDPnKLRGIAVKRGMmdedaaarltdkecfnl 548
Cdd:cd16924    9 LVENAIQHGLSP--------LTDKGVVTISALKEDNHVMIEVEDNGRGIDP-KVLNILGKKPK----------------- 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875 549 ifapgfsskdkisdiSGRGVGMDVVKTAINTLNG---SIDIDSELGKGTKITIKVP 601
Cdd:cd16924   63 ---------------EGNGIGLYNVHQRLILLFGedyGIHIASEPDKGTRITFTIP 103
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
610-737 6.63e-06

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 46.40  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 610 LMVGVGGHPFALPLASVSEIFHL-DLSR----TNVVDGqlTIIVREKSIPLFYLQNWLASKSQNVQERTghgHVVIVQIG 684
Cdd:COG0835   11 LTFRLGGERYAIPIEKVREILPLpPITPvpgaPPWVLG--VINLRGRVVPVIDLRALLGLPPTEDTERT---RIIVLEVG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491522875 685 NQRVGFVVDTLIGQEEV----VIKPLDNLLQGTPGMAGATITSDGHIALILDVPDLL 737
Cdd:COG0835   86 GRVVGLLVDSVSGVVRIdpddIEPPPELLSGGLAPFITGVAKLDDRLILLLDLEKLL 142
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
430-603 9.60e-05

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 44.61  E-value: 9.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 430 RVVRDLARNLNKDIVLEMRGEETDLDKNLVEALAdpLI--HLVRNSVDHgiempdARAKagksrtgKVILSASQEGDHIE 507
Cdd:COG4585  131 ELAERLLRAAGIRVELDVDGDPDRLPPEVELALY--RIvqEALTNALKH------AGAT-------RVTVTLEVDDGELT 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 508 LSIVDDGGGMDPNKlrgiavkrgmmdedaaarltdkecfnlifapgfsskdkisdISGRGVGMDVVKTAINTLNGSIDID 587
Cdd:COG4585  196 LTVRDDGVGFDPEA-----------------------------------------APGGGLGLRGMRERAEALGGTLTIG 234

                        170
                 ....*....|....*.
gi 491522875 588 SELGKGTKITIKVPLT 603
Cdd:COG4585  235 SAPGGGTRVRATLPLA 250
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 493-602 1.31e-04

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: 41.54  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 493 GKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPGF---SSKDKISdiSGRGVG 569
Cdd:cd16949   18 SKILLDISQDGDQWTITITDDGPGVPEDQL------------------------EQIFLPFYrvdSARDRES--GGTGLG 71

                         90       100       110
                 ....*....|....*....|....*....|...
gi 491522875 570 MDVVKTAINTLNGSIDIDSELGKGTKITIKVPL 602
Cdd:cd16949   72 LAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
469-534 2.22e-04

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 41.44  E-value: 2.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491522875 469 LVRNSVDHGiempdarakAGKSRTGKVILSASQEGDHIELSIVDDGGGMDPNKL-----------RGIAVKRGMMDE 534
Cdd:COG2172   42 AVTNAVRHA---------YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLpdpystlaeggRGLFLIRRLMDE 109
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 502-601 2.67e-04

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: 41.21  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 502 EGDHIELSIVDDGGGMDPnklrgiavkrgmmdedaaarltdkECFNLIFAPGFSSKDKISdisGRGVGMDVVKTAINTLN 581
Cdd:cd16919   44 PGNYVCLEVSDTGSGMPA------------------------EVLRRAFEPFFTTKEVGK---GTGLGLSMVYGFVKQSG 96

                         90       100
                 ....*....|....*....|
gi 491522875 582 GSIDIDSELGKGTKITIKVP 601
Cdd:cd16919   97 GHLRIYSEPGVGTTVRIYLP 116
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 468-601 7.31e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 39.88  E-value: 7.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 468 HLVRNSVDHgieMPDArakagksrtGKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaARLTDKecFN 547
Cdd:cd16952    7 NLVSNAVKY---TPPS---------DTITVRWSQEESGARLSVEDTGPGIPPEHI---------------PRLTER--FY 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491522875 548 LIfapgfsSKDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVP 601
Cdd:cd16952   58 RV------DIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFP 105
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
492-611 1.22e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 42.27  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 492 TGKVILSASQEGDHIELSIVDDGGGMDPnklrgiavkrgmmdedaaarltdKECFNLiFAPGFS-SKDKISDISGRGVGM 570
Cdd:PRK10841 580 TGCIVLHVRVDGDYLSFRVRDTGVGIPA-----------------------KEVVRL-FDPFFQvGTGVQRNFQGTGLGL 635

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491522875 571 DVVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLM 611
Cdd:PRK10841 636 AICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKK 676
PRK15347 PRK15347
two component system sensor kinase;
492-624 1.73e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 41.94  E-value: 1.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 492 TGKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPGFSSKDkisDISGRGVGMD 571
Cdd:PRK15347 531 TGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQ------------------------QQIFTPFYQADT---HSQGTGLGLT 583

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491522875 572 VVKTAINTLNGSIDIDSELGKGTKITIKVPLTLAILPTLMVGvgghPFALPLA 624
Cdd:PRK15347 584 IASSLAKMMGGELTLFSTPGVGSCFSLVLPLNEYAPPEPLKG----ELSAPLA 632
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 466-601 1.79e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 38.53  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 466 LIHLVRNsvdhGIEmpdARAKAGKSRTGKVILSASQEGDHIELSIVDDGGGMDpnklrgiavkrgmmdEDAAARLtdkec 545
Cdd:cd16920    5 LINLVRN----GIE---AMSEGGCERRELTIRTSPADDRAVTISVKDTGPGIA---------------EEVAGQL----- 57

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875 546 fnliFAPGFSSKdkisdISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVP 601
Cdd:cd16920   58 ----FDPFYTTK-----SEGLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
466-603 3.43e-03

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 40.82  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 466 LIHLVRNSVdHGIEMP---DARAKAGKSRTGKVILSAS-QEGDHIELSIVDDGGGMDPNKLRGIavkrgmmdedaaarlt 541
Cdd:PRK13837 565 LMNLCSNAA-QAMDGAgrvDISLSRAKLRAPKVLSHGVlPPGRYVLLRVSDTGAGIDEAVLPHI---------------- 627

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491522875 542 dkecfnliFAPGFSSKDkisdiSGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPLT 603
Cdd:PRK13837 628 --------FEPFFTTRA-----GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPS 676
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 441-518 5.57e-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: 37.78  E-value: 5.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491522875 441 KDIVLEMRGEETDLDKNLVEALADPLIHLVRNSVDHGIempDARAkagksrTGKVILSASQEGDHIELSIVDDGGGMD 518
Cdd:cd16951   19 GDIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAF---SDRE------GGTITIRSVVDGDYLRITVIDDGVGLP 87
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 466-601 7.66e-03

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


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 36.66  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 466 LIHLVRNSVDHGiempdarakagksrTGKVILSASQEGDHIELSIVDDGGGMDPNKLrgiavkrgmmDEdaaarltdkec 545
Cdd:cd16950    5 LSNLVDNALRYG--------------GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEV----------DE----------- 49

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491522875 546 fnlIFAPgFSSKDKISDISGRGVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVP 601
Cdd:cd16950   50 ---LFQP-FYRGDNARGTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 493-602 9.59e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 36.32  E-value: 9.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491522875 493 GKVILSAS-----QEGDHIELSIVDDGGGMDPNKLrgiavkrgmmdedaaarltdkecfNLIFAPgFSSKDkiSDISGR- 566
Cdd:cd16922   19 GEVTLRVSleeeeEDGVQLRFSVEDTGIGIPEEQQ------------------------ARLFEP-FSQAD--SSTTRKy 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 491522875 567 ---GVGMDVVKTAINTLNGSIDIDSELGKGTKITIKVPL 602
Cdd:cd16922   72 ggtGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
 
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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