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Conserved domains on  [gi|2308515618|ref|WP_261217428|]
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chemotaxis protein CheA [Arcobacter lacus]

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];
4-671 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 586.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   4 DISKYREMFLEEAVELFESADNVLLEAENNGSlTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIE 83
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLLALEQDPD-DPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  84 FVPEMAGTLIDGLDVMKEILDLEVADQMTREKFvemtSSLLEdiraysngtavqkvetpKIEEKKKEIPSVNSsdkenfg 163
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPADI----SALLA-----------------RLDASEEAIEEVVA------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 164 ffdnglneqrdnknqpygifadddineeqknygffddnlekksdnlndddfkldnnkedfgffddmpsispdsvmktndi 243
Cdd:COG0643       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 244 EEQKIETPSTIQKETEIATKKPKTTTNNTEDEAKKVASnnnnSIRVNLDKIDLLMNNVGDLVITNAMLTQFSSTIEETKT 323
Cdd:COG0643   133 DEVEISPPAPAALEPAPAAAPPAEAAAAAAEAAAAASE----TVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESL 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 324 RgSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDPLMHIIR 403
Cdd:COG0643   209 R-ELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVR 287

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 404 NSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQKALEKGQIDENQYNAMTNNEKALLIFG 483
Cdd:COG0643   288 NAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFA 367

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 484 AGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLTLAILDGLDIRVANQKYILPLSSIVESLQ 563
Cdd:COG0643   368 PGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR 447

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 564 PTADMIKKIGDgtQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSGNTKVALSIDEFLNQHQVVVKPLDKNFR 643
Cdd:COG0643   448 LDPDDIETVEG--REVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLR 525

                         650       660
                  ....*....|....*....|....*...
gi 2308515618 644 SVQGIGAATVKGDGSIGLILDVVGIINA 671
Cdd:COG0643   526 RVPGISGATILGDGRVALILDVAALVRS 553
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
4-671 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 586.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   4 DISKYREMFLEEAVELFESADNVLLEAENNGSlTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIE 83
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLLALEQDPD-DPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  84 FVPEMAGTLIDGLDVMKEILDLEVADQMTREKFvemtSSLLEdiraysngtavqkvetpKIEEKKKEIPSVNSsdkenfg 163
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPADI----SALLA-----------------RLDASEEAIEEVVA------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 164 ffdnglneqrdnknqpygifadddineeqknygffddnlekksdnlndddfkldnnkedfgffddmpsispdsvmktndi 243
Cdd:COG0643       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 244 EEQKIETPSTIQKETEIATKKPKTTTNNTEDEAKKVASnnnnSIRVNLDKIDLLMNNVGDLVITNAMLTQFSSTIEETKT 323
Cdd:COG0643   133 DEVEISPPAPAALEPAPAAAPPAEAAAAAAEAAAAASE----TVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESL 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 324 RgSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDPLMHIIR 403
Cdd:COG0643   209 R-ELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVR 287

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 404 NSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQKALEKGQIDENQYNAMTNNEKALLIFG 483
Cdd:COG0643   288 NAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFA 367

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 484 AGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLTLAILDGLDIRVANQKYILPLSSIVESLQ 563
Cdd:COG0643   368 PGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR 447

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 564 PTADMIKKIGDgtQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSGNTKVALSIDEFLNQHQVVVKPLDKNFR 643
Cdd:COG0643   448 LDPDDIETVEG--REVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLR 525

                         650       660
                  ....*....|....*....|....*...
gi 2308515618 644 SVQGIGAATVKGDGSIGLILDVVGIINA 671
Cdd:COG0643   526 RVPGISGATILGDGRVALILDVAALVRS 553
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 4-665 1.99e-155

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 464.59  E-value: 1.99e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   4 DISKYREMFLEEAVELFESADNVLLEAenNGSLTDDE-MGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKI 82
Cdd:PRK10547    2 DISDFYQTFFDEADELLADMEQHLLVL--DPEAPDAEqLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  83 EFVPEMAGTLIDGLDVMKEILD-LEVADQMTREKFVEMTSSL----LEdirAYSNGTAVQKVETPKIEEKKKEIPSVNSS 157
Cdd:PRK10547   80 QLNTDIINLFLETKDIMQEQLDaYKTSQEPDAASFEYICQALrqlaLE---AKGETPSAVTRLSVVAIQEKSEPQDESPR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 158 DKENFGFFDNGLNEQrdnknqpygifaddDIN---EEQKNYGFFDDnLEKKSDNL--------NDDD------FKLDNNK 220
Cdd:PRK10547  157 SQSGLRIILSRLKAG--------------EVDlleEELGNLGTLTD-VVKGADSLeatlpgsvAEDDitavlcFVIEADQ 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 221 EDFGFFDDMPSISPDSVMKTNDIEEQKIETPSTIQKETEIATKKPKtttnntedEAKKVASNNNNSIRVNLDKIDLLMNN 300
Cdd:PRK10547  222 ITFETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAGRVE--------REKTARSSESTSIRVAVEKVDQLINL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 301 VGDLVITNAMLTQFSSTIEETKtRGSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNKKVEFKHY 380
Cdd:PRK10547  294 VGELVITQSMLAQRSSELDPVN-HGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLV 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 381 GDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQKALE 460
Cdd:PRK10547  373 GSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAAS 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 461 KG-QIDENqynaMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLTLAIL 539
Cdd:PRK10547  453 QGlAVSEN----MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAIL 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 540 DGLDIRVANQKYILPLSSIVESLQPTADMIKKIGdGTQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSGNTK 619
Cdd:PRK10547  529 DGMSVRVADEVFILPLNAVMESLQPREEDLHPLA-GGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRR 607

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 2308515618 620 VALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKGDGSIGLILDV 665
Cdd:PRK10547  608 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDV 653
CheA_Halo NF041336
chemotaxis protein CheA;
6-666 3.22e-99

chemotaxis protein CheA;


Pssm-ID: 469233 [Multi-domain]  Cd Length: 666  Bit Score: 318.91  E-value: 3.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   6 SKYREMFLEEAVELFESADNVLLEAENNGSlTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIEFV 85
Cdd:NF041336    2 DDYLDAFVRESEEAITELNNSLLELESDPE-NEEAMETIFRTAHTLKGNFGAMGFDDASNLAHAIEDLLDEIRQGELAVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  86 PEMAGTLIDGLDVMKEILDlEVADqmTREKFVEmTSSLLEDIRAYSNGTAVQKVEtpkieEKKKEIPSVNSSDkeNFGFF 165
Cdd:NF041336   81 PERMDLIFEGVDQLEAIVD-EIEA--DGETQTD-PEATIEEIRASIEEGADAGAS-----GAVEDGDAGDSSA--DDGIV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 166 DNGLNEQR-------------------DNKNQPY--GIFADDDINEEqknYGFFDdnLEKKSDNLNDDDF---------- 214
Cdd:NF041336  150 DADVVVDDvvvpelaadgevyharveiGDSDMPGvdAMLVLEAIEDE---FDLLG--TVPDRDAIEDGEFedtfdlyvat 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 215 KLDNNKEDF-GFFDDMPSISPDSVMKTNDIEEqkieTPSTIQKETEIATKKPKTTTNNTEDEAKKVASNNNNSIRVNLDK 293
Cdd:NF041336  225 DNDVDSDDVeAFYELNGYVDTVDVEDVTDEVA----AGDLKDGPTEDDDDAGADTDDSGSSSSMAHSVQEIESVRVDVDQ 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 294 IDLLMNNVGDLVITNAMLTQfsstIEETKTRGSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNK 373
Cdd:NF041336  301 LDQLYGLVEQLVTSRIKLRR----AVEEEDLVSAEDELEELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGK 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 374 KVEFKHYGDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSER 453
Cdd:NF041336  377 EIDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEE 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 454 VAQKALEKGQIDENQYNAMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:NF041336  457 IREKAIEKGVKTEEELEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLP 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 534 LTLAILDGLDIRVANQKYILPLSSIVESLQptADMIKKIgDGTQdLLMLREEFIPVVKLHQLFGLEKSfEKLEDGMLIVV 613
Cdd:NF041336  537 VTVAIVKVLFVTVGDEEYGIPIKNVDEISR--LEDVETV-NGRE-VITHDDEIYPLVSLGDALDVPGE-TRNGDGMLVRI 611

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 614 KSGNTKVALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKGDGSIGLILDVV 666
Cdd:NF041336  612 RESERQVALHCDDVVGQEEVVVKPFEGILSGTPGLSGTAVLGDGEVVHILDVV 664
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 356-533 1.52e-76

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: 242.87  E-value: 1.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 356 IYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQAN 435
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 436 GQMIITIQDDGKGIDSERVAQKALEKGQIDENQYNAMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGV 515
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 2308515618 516 INLDTEIGKGTTITIMLP 533
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheW smart00260
Two component signalling adaptor domain;
529-669 5.34e-24

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 98.08  E-value: 5.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  529 TIMLPLTLAILDGldirvanQKYILPLSSIVESLQPT-ADMIKKIGDGTQDLLMLREEFIPVVKLHQLFGLEkSFEKLED 607
Cdd:smart00260   1 TIRLPLTFAIGKD-------ETYAIPIAAVREILRPPpITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLP-PEPPTDE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618  608 GMLIVVKSGNTKVALSIDEFLNQHQVVVKPLDK----NFRSVQGIGAATVKGDGSIGLILDVVGII 669
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKLL 138
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 541-668 7.31e-21

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: 88.80  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 541 GLDIRVANQKYILPLSSIVESLQPTA-DMIKKIGDGTQDLLMLREEFIPVVKLHQLFGLEKSfEKLEDGMLIVVKSGNTK 619
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPiTPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPT-EPRERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2308515618 620 VALSIDEFLNQHQVVVKPLDKNFRSVQGIG---AATVKGDGSIGLILDVVGI 668
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLGLGRVAGyisGATILGDGRVVLILDVEAL 131
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
4-671 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 586.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   4 DISKYREMFLEEAVELFESADNVLLEAENNGSlTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIE 83
Cdd:COG0643     2 DMDELLEIFLEEARELLEQLEEGLLALEQDPD-DPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  84 FVPEMAGTLIDGLDVMKEILDLEVADQMTREKFvemtSSLLEdiraysngtavqkvetpKIEEKKKEIPSVNSsdkenfg 163
Cdd:COG0643    81 LTPELIDLLLEALDALRALLDALEAGGEPPADI----SALLA-----------------RLDASEEAIEEVVA------- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 164 ffdnglneqrdnknqpygifadddineeqknygffddnlekksdnlndddfkldnnkedfgffddmpsispdsvmktndi 243
Cdd:COG0643       --------------------------------------------------------------------------------

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 244 EEQKIETPSTIQKETEIATKKPKTTTNNTEDEAKKVASnnnnSIRVNLDKIDLLMNNVGDLVITNAMLTQFSSTIEETKT 323
Cdd:COG0643   133 DEVEISPPAPAALEPAPAAAPPAEAAAAAAEAAAAASE----TVRVDVERLDRLMNLVGELVITRARLEQLAEELEDESL 208

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 324 RgSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDPLMHIIR 403
Cdd:COG0643   209 R-ELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVR 287

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 404 NSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQKALEKGQIDENQYNAMTNNEKALLIFG 483
Cdd:COG0643   288 NAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAAALSDEELLELIFA 367

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 484 AGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLTLAILDGLDIRVANQKYILPLSSIVESLQ 563
Cdd:COG0643   368 PGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR 447

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 564 PTADMIKKIGDgtQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSGNTKVALSIDEFLNQHQVVVKPLDKNFR 643
Cdd:COG0643   448 LDPDDIETVEG--REVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLR 525

                         650       660
                  ....*....|....*....|....*...
gi 2308515618 644 SVQGIGAATVKGDGSIGLILDVVGIINA 671
Cdd:COG0643   526 RVPGISGATILGDGRVALILDVAALVRS 553
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 4-665 1.99e-155

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 464.59  E-value: 1.99e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   4 DISKYREMFLEEAVELFESADNVLLEAenNGSLTDDE-MGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKI 82
Cdd:PRK10547    2 DISDFYQTFFDEADELLADMEQHLLVL--DPEAPDAEqLNAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  83 EFVPEMAGTLIDGLDVMKEILD-LEVADQMTREKFVEMTSSL----LEdirAYSNGTAVQKVETPKIEEKKKEIPSVNSS 157
Cdd:PRK10547   80 QLNTDIINLFLETKDIMQEQLDaYKTSQEPDAASFEYICQALrqlaLE---AKGETPSAVTRLSVVAIQEKSEPQDESPR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 158 DKENFGFFDNGLNEQrdnknqpygifaddDIN---EEQKNYGFFDDnLEKKSDNL--------NDDD------FKLDNNK 220
Cdd:PRK10547  157 SQSGLRIILSRLKAG--------------EVDlleEELGNLGTLTD-VVKGADSLeatlpgsvAEDDitavlcFVIEADQ 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 221 EDFGFFDDMPSISPDSVMKTNDIEEQKIETPSTIQKETEIATKKPKtttnntedEAKKVASNNNNSIRVNLDKIDLLMNN 300
Cdd:PRK10547  222 ITFETAVAAPQEKAEETTEVVEVSPKISVPPVLKLAAEQAPAGRVE--------REKTARSSESTSIRVAVEKVDQLINL 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 301 VGDLVITNAMLTQFSSTIEETKtRGSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNKKVEFKHY 380
Cdd:PRK10547  294 VGELVITQSMLAQRSSELDPVN-HGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLV 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 381 GDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQKALE 460
Cdd:PRK10547  373 GSSTELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAAS 452

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 461 KG-QIDENqynaMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLTLAIL 539
Cdd:PRK10547  453 QGlAVSEN----MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAIL 528

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 540 DGLDIRVANQKYILPLSSIVESLQPTADMIKKIGdGTQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSGNTK 619
Cdd:PRK10547  529 DGMSVRVADEVFILPLNAVMESLQPREEDLHPLA-GGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRR 607

                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 2308515618 620 VALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKGDGSIGLILDV 665
Cdd:PRK10547  608 YALLVDQLIGQHQVVVKNLESNYRKVPGISAATILGDGSVALIVDV 653
CheA_Halo NF041336
chemotaxis protein CheA;
6-666 3.22e-99

chemotaxis protein CheA;


Pssm-ID: 469233 [Multi-domain]  Cd Length: 666  Bit Score: 318.91  E-value: 3.22e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   6 SKYREMFLEEAVELFESADNVLLEAENNGSlTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIEFV 85
Cdd:NF041336    2 DDYLDAFVRESEEAITELNNSLLELESDPE-NEEAMETIFRTAHTLKGNFGAMGFDDASNLAHAIEDLLDEIRQGELAVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  86 PEMAGTLIDGLDVMKEILDlEVADqmTREKFVEmTSSLLEDIRAYSNGTAVQKVEtpkieEKKKEIPSVNSSDkeNFGFF 165
Cdd:NF041336   81 PERMDLIFEGVDQLEAIVD-EIEA--DGETQTD-PEATIEEIRASIEEGADAGAS-----GAVEDGDAGDSSA--DDGIV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 166 DNGLNEQR-------------------DNKNQPY--GIFADDDINEEqknYGFFDdnLEKKSDNLNDDDF---------- 214
Cdd:NF041336  150 DADVVVDDvvvpelaadgevyharveiGDSDMPGvdAMLVLEAIEDE---FDLLG--TVPDRDAIEDGEFedtfdlyvat 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 215 KLDNNKEDF-GFFDDMPSISPDSVMKTNDIEEqkieTPSTIQKETEIATKKPKTTTNNTEDEAKKVASNNNNSIRVNLDK 293
Cdd:NF041336  225 DNDVDSDDVeAFYELNGYVDTVDVEDVTDEVA----AGDLKDGPTEDDDDAGADTDDSGSSSSMAHSVQEIESVRVDVDQ 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 294 IDLLMNNVGDLVITNAMLTQfsstIEETKTRGSVLERLELLERHIRDMQDSIMSIRMVPMDSIYSKFPKVVRDISKKLNK 373
Cdd:NF041336  301 LDQLYGLVEQLVTSRIKLRR----AVEEEDLVSAEDELEELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGK 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 374 KVEFKHYGDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSER 453
Cdd:NF041336  377 EIDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEE 456

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 454 VAQKALEKGQIDENQYNAMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:NF041336  457 IREKAIEKGVKTEEELEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLP 536

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 534 LTLAILDGLDIRVANQKYILPLSSIVESLQptADMIKKIgDGTQdLLMLREEFIPVVKLHQLFGLEKSfEKLEDGMLIVV 613
Cdd:NF041336  537 VTVAIVKVLFVTVGDEEYGIPIKNVDEISR--LEDVETV-NGRE-VITHDDEIYPLVSLGDALDVPGE-TRNGDGMLVRI 611

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 614 KSGNTKVALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKGDGSIGLILDVV 666
Cdd:NF041336  612 RESERQVALHCDDVVGQEEVVVKPFEGILSGTPGLSGTAVLGDGEVVHILDVV 664
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 356-533 1.52e-76

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: 242.87  E-value: 1.52e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 356 IYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDPLMHIIRNSLDHGIEMPEDRVALGKIETGSISISAEQAN 435
Cdd:cd16916     1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 436 GQMIITIQDDGKGIDSERVAQKALEKGQIDENQYNAMTNNEKALLIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGV 515
Cdd:cd16916    81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAATLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                         170
                  ....*....|....*...
gi 2308515618 516 INLDTEIGKGTTITIMLP 533
Cdd:cd16916   161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 536-668 2.73e-39

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: 141.16  E-value: 2.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 536 LAILDGLDIRVANQKYILPLSSIVESLQPTADMIKKIgDGTQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKS 615
Cdd:cd00731     1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRV-DGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRT 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 616 GNTKVALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKGDGSIGLILDVVGI 668
Cdd:cd00731    80 GGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
CheW smart00260
Two component signalling adaptor domain;
529-669 5.34e-24

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 98.08  E-value: 5.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  529 TIMLPLTLAILDGldirvanQKYILPLSSIVESLQPT-ADMIKKIGDGTQDLLMLREEFIPVVKLHQLFGLEkSFEKLED 607
Cdd:smart00260   1 TIRLPLTFAIGKD-------ETYAIPIAAVREILRPPpITPIPGAPGYVLGVINLRGEVLPVVDLRRLLGLP-PEPPTDE 72

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618  608 GMLIVVKSGNTKVALSIDEFLNQHQVVVKPLDK----NFRSVQGIGAATVKGDGSIGLILDVVGII 669
Cdd:smart00260  73 TRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGDGRVVLILDVDKLL 138
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 541-668 7.31e-21

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: 88.80  E-value: 7.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 541 GLDIRVANQKYILPLSSIVESLQPTA-DMIKKIGDGTQDLLMLREEFIPVVKLHQLFGLEKSfEKLEDGMLIVVKSGNTK 619
Cdd:pfam01584   1 GLLFRLGGETFAIPISKVREILRPPPiTPIPGAPGYVLGVINLRGEVLPVIDLRRLLGLPPT-EPRERTRVVVVEVGGQV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2308515618 620 VALSIDEFLNQHQVVVKPLDKNFRSVQGIG---AATVKGDGSIGLILDVVGI 668
Cdd:pfam01584  80 VGLLVDEVIGVLEIVIKQIEPPLGLGRVAGyisGATILGDGRVVLILDVEAL 131
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 393-535 1.75e-20

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 86.93  E-value: 1.75e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618  393 GLTDPLMHIIRNSLDHGIE-MPEDrvalgkietGSISISAEQANGQMIITIQDDGKGIDSERVAQkalekgqidenqyna 471
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKyTPEG---------GRITVTLERDGDHVEITVEDNGPGIPPEDLEK--------------- 56

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2308515618  472 mtnnekallIFGAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLT 535
Cdd:smart00387  57 ---------IFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 538-668 9.53e-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: 85.79  E-value: 9.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 538 ILDGLDIRVANQKYILPLSSIVESLQPTADM-IKKIGDGTQDLLMLREEFIPVVKLHQLFGLEKSFEKLEDGMLIVVKSG 616
Cdd:cd00588     1 ILQVLLFRVGDELYAIPIAVVEEILPLPPITrVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618 617 NTKVALSIDEFLNQHQVVVKPLDKNF----RSVQGIGAATVKGDGSIGLILDVVGI 668
Cdd:cd00588    81 DRKVGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 8-100 2.06e-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: 74.98  E-value: 2.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618    8 YREMFLEEAVELFESADNVLLEAENNgsLTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHKIEFVPE 87
Cdd:smart00073   2 GLELFREELAEFLQSLEEGLLELEKA--LDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 2308515618   88 MAGTLIDGLDVMK 100
Cdd:smart00073  80 LLDLLLELVDVLK 92
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 5-104 4.59e-16

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: 73.95  E-value: 4.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   5 ISKYREMFLEEAVELFESADNVLLEAENngsltDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLMDKLRSHkIEF 84
Cdd:cd00088     1 MEELLELFLEEAEELLEELERALLELED-----AEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEV 74

                          90       100
                  ....*....|....*....|
gi 2308515618  85 VPEMAGTLIDGLDVMKEILD 104
Cdd:cd00088    75 TPELIDLLLDALDALKAELE 94
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 286-348 7.14e-16

Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the homodimer interface of the signal transducing histidine kinase family.


Pssm-ID: 427045 [Multi-domain]  Cd Length: 66  Bit Score: 72.27  E-value: 7.14e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618 286 SIRVNLDKIDLLMNNVGDLVITNAMLTQFSSTIEETKTRGSV---LERLELLERHIRDMQDSIMSI 348
Cdd:pfam02895   1 TIRVDVEKLDRLMNLVGELVIARNRLVQLLERLEEYGGDTLLeelKEALQQLDRLTRELQEAVMKI 66
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
326-535 2.51e-14

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 74.56  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 326 SVLERLELLERHIRDMQD------SIMSIRMVPMDsiyskFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDP-- 397
Cdd:COG0642   149 TILRSADRLLRLINDLLDlsrleaGKLELEPEPVD-----LAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPdr 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 398 ----LMHIIRNSLDHgieMPEDrvalgkietGSISISAEQANGQMIITIQDDGKGIDSERVAQkalekgqidenqynamt 473
Cdd:COG0642   224 lrqvLLNLLSNAIKY---TPEG---------GTVTVSVRREGDRVRISVEDTGPGIPPEDLER----------------- 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2308515618 474 nnekallIFGAGiSTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLT 535
Cdd:COG0642   275 -------IFEPF-FRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 393-535 3.14e-13

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: 66.24  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 393 GLTDPLMHIIRNSLDHGIEmpedrvALGKIETGSISISAEqanGQMIITIQDDGKGIDSERVAQkalekgqidenqynam 472
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALK------HAAKAGEITVTLSEG---GELTLTVEDNGIGIPPEDLPR---------------- 55

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 473 tnnekallIFGAGiSTADKiTDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLT 535
Cdd:pfam02518  56 --------IFEPF-STADK-RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
285-535 4.49e-13

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 69.17  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 285 NSIRVNLDkidLLMNNVGdlvITNAMLTQFSSTIEETKTRgsvLERL--ELLErhIRDMQDSIMSIRMVPMDsiyskFPK 362
Cdd:COG2205    32 TSILGAAE---LLLDEED---LSPEERRELLEIIRESAER---LLRLieDLLD--LSRLESGKLSLELEPVD-----LAE 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 363 VVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTDP--LMHIIRNSLDHGIE-MPEDrvalgkietGSISISAEQANGQMI 439
Cdd:COG2205    96 LLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPelLEQVLANLLDNAIKySPPG---------GTITISARREGDGVR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 440 ITIQDDGKGIDSERVAQkalekgqidenqynamtnnekallIFgAGISTADKITDISGRGVGMDVVKTNIHKLGGVINLD 519
Cdd:COG2205   167 ISVSDNGPGIPEEELER------------------------IF-ERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVE 221

                         250
                  ....*....|....*.
gi 2308515618 520 TEIGKGTTITIMLPLT 535
Cdd:COG2205   222 SEPGGGTTFTVTLPLA 237
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 387-533 1.32e-12

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 70.71  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 387 DKAMIEGLTDPLMHIIRNSLDhgiempedrvALGKIETGSISISAEQANGQMIITIQDDGKGIDSERVAQkalekgqide 466
Cdd:PRK11086  427 DEDQVHELITILGNLIENALE----------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDA---------- 486

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2308515618 467 nqynamtnnekallIFGAGISTADKitdisGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:PRK11086  487 --------------IFDKGYSTKGS-----NRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 318-535 2.77e-11

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 65.59  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 318 IEETKTRGSVLERLELLERHIRDMQDSIMSIR---------MVPMDsiyskFPKVVRDIS-------KKLNKKVEfKHYG 381
Cdd:COG4191   171 LEDEPDPEELREALERILEGAERAAEIVRSLRafsrrdeeeREPVD-----LNELIDEALellrprlKARGIEVE-LDLP 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 382 DN---VEIDKAMIEGLtdpLMHIIRNSLDhgiempedrvALGKIETGSISISAEQANGQMIITIQDDGKGIDSErvaqkA 458
Cdd:COG4191   245 PDlppVLGDPGQLEQV---LLNLLINAID----------AMEEGEGGRITISTRREGDYVVISVRDNGPGIPPE-----V 306

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 459 LEKgqidenqynamtnnekallIF-------GAGistadkitdiSGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIM 531
Cdd:COG4191   307 LER-------------------IFepffttkPVG----------KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357


                  ....
gi 2308515618 532 LPLT 535
Cdd:COG4191   358 LPLA 361
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 7-97 4.82e-11

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: 59.29  E-value: 4.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618   7 KYREMFLEEAVELFESADNvlleaenngSLTDDEMGQLFRDVHTLKGSGASVELAFFAEFTHDVENLmdkLRSHKIEFVP 86
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQ---------ALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDP 68

                          90
                  ....*....|.
gi 2308515618  87 EMAGTLIDGLD 97
Cdd:pfam01627  69 ELLEALRDLLE 79
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 373-537 3.69e-09

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 59.09  E-value: 3.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 373 KKVEFkhygdNVEIDKAMIEGLTDP--LMHIIRNSLDHGIEmpedrvALGKIETG--SISISAEQANGQMIITIQDDGKG 448
Cdd:COG3290   260 RGIDL-----TIDIDSDLPDLPLSDtdLVTILGNLLDNAIE------AVEKLPEEerRVELSIRDDGDELVIEVEDSGPG 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 449 IDSERVAQkalekgqidenqynamtnnekallIFGAGISTADKitdiSGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTI 528
Cdd:COG3290   329 IPEELLEK------------------------IFERGFSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVF 380


                  ....*....
gi 2308515618 529 TIMLPLTLA 537
Cdd:COG3290   381 TVRLPKEGE 389
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 384-535 9.74e-08

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: 54.97  E-value: 9.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 384 VEIDKAMIEGLtdpLMHIIRNSLDhgiempedrvALGkiETGSISISAEQANGQMIITIQDDGKGIDSErVAQKALEkgq 463
Cdd:COG5000   311 VLADRDQLEQV---LINLLKNAIE----------AIE--EGGEIEVSTRREDGRVRIEVSDNGPGIPEE-VLERIFE--- 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2308515618 464 idenQYnaMTNNEKallifgagistadkitdisGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPLT 535
Cdd:COG5000   372 ----PF--FTTKPK-------------------GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLA 418
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 398-533 1.84e-07

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: 49.59  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 398 LMHIIRNSLDHGIempeDRVALGKIETGSISISAEQANGQMIITIQDDGKGIDSErvaqkalekgqidenqynamtnneK 477
Cdd:cd16915     1 LITIVGNLIDNAL----DALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPE------------------------L 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618 478 ALLIFGAGISTADKitdiSGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:cd16915    53 RDKVFERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 384-533 3.84e-07

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 53.25  E-value: 3.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 384 VEIDKAMIEGLtdpLMHIIRNSLDHGiempedrvalGKIETGSISISAEQANGQMIITIQDDGKGIDservaQKALEKgq 463
Cdd:COG4251   388 VRGDPTLLRQV---FQNLISNAIKYS----------RPGEPPRIEIGAEREGGEWVFSVRDNGIGID-----PEYAEK-- 447

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 464 idenqynamtnnekallIFGAgISTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:COG4251   448 -----------------IFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 401-533 9.74e-07

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: 47.43  E-value: 9.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 401 IIRNSLDHGIEmpedrvalGKIETGSISISAEQANGQMIITIQDDGKGIDSErvaqkALEKGQIDENQYNAMTNnekall 480
Cdd:cd16956     9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMDPD-----TLARILIRSSNGLGLNL------ 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 481 ifgagisTADKITDISGRGVGMDVvktnihklggvinlDTEIGKGTTITIMLP 533
Cdd:cd16956    70 -------VDKRLRQAFGNDYGLDI--------------ECAPGEGTRITIRLP 101
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 372-535 1.11e-06

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 51.66  E-value: 1.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 372 NKKVEFKHYGD--NVEIDKAMIEGLtdpLMHIIRNSLDhgiEMPEDrvalgkietGSISISAEQANGQMIITIQDDGKGI 449
Cdd:COG5805   375 NIQIRLELLDEdpFIYCDENQIKQV---FINLIKNAIE---AMPNG---------GTITIHTEEEDNSVIIRVIDEGIGI 439

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 450 DSERvaqkaLEKgqIDENQYnamTNNEKallifgagistadkitdisGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTIT 529
Cdd:COG5805   440 PEER-----LKK--LGEPFF---TTKEK-------------------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFT 490


                  ....*.
gi 2308515618 530 IMLPLT 535
Cdd:COG5805   491 ITLPLS 496
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
329-534 3.74e-06

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 49.94  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 329 ERLELLerhIRDMQD------SIMSIRMVPMDsiyskFPKVVRDISKKLNKKVEFKHYGDNVEI--DKAMIEGLTDPLMH 400
Cdd:COG5002   213 ERLSRL---VNDLLDlsrlesGELKLEKEPVD-----LAELLEEVVEELRPLAEEKGIELELDLpeDPLLVLGDPDRLEQ 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 401 IIRNSLDHGIE-MPEDrvalgkietGSISISAEQANGQMIITIQDDGKGIDSErvaqkALEKgqidenqynamtnnekal 479
Cdd:COG5002   285 VLTNLLDNAIKyTPEG---------GTITVSLREEDDQVRISVRDTGIGIPEE-----DLPR------------------ 332

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2308515618 480 lIFGAgISTADK--ITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPL 534
Cdd:COG5002   333 -IFER-FYRVDKsrSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
362-535 5.79e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 49.07  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 362 KVVRDISKKLNKKVEFK-HYGDN---VEIDKAMIEGLtdpLMHIIRNSLDhgiempedrvALGkiETGSISISAEQANGQ 437
Cdd:COG3852   212 RVLELLRAEAPKNIRIVrDYDPSlpeVLGDPDQLIQV---LLNLVRNAAE----------AMP--EGGTITIRTRVERQV 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 438 MI----------ITIQDDGKGIDSErvaqkALEKgqidenqynamtnnekallIFGAGISTADKitdisGRGVGMDVVKT 507
Cdd:COG3852   277 TLgglrprlyvrIEVIDNGPGIPEE-----ILDR-------------------IFEPFFTTKEK-----GTGLGLAIVQK 327

                         170       180
                  ....*....|....*....|....*...
gi 2308515618 508 NIHKLGGVINLDTEIGKGTTITIMLPLT 535
Cdd:COG3852   328 IVEQHGGTIEVESEPGKGTTFRIYLPLE 355
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 372-535 1.19e-05

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 48.36  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 372 NKKVEFKHYGDNVEI--DKAMIEGLtdpLMH-IIRNSLDHGiempedrvALGKiETGSISISAEQANGQMIITIQDDGKG 448
Cdd:COG3920   378 GRGIRIELDGPDVELpaDAAVPLGL---ILNeLVTNALKHA--------FLSG-EGGRIRVSWRREDGRLRLTVSDNGVG 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 449 IDSErvaqkalekgqidenqynamtnnekallifgagistadkITDISGRGVGMDVVKTNIHKLGGVINLDTEigKGTTI 528
Cdd:COG3920   446 LPED---------------------------------------VDPPARKGLGLRLIRALVRQLGGTLELDRP--EGTRV 484


                  ....*..
gi 2308515618 529 TIMLPLT 535
Cdd:COG3920   485 RITFPLA 491
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
423-534 1.94e-05

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 47.66  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 423 ETGSISISAEQ-ANGQMIITIQDDGKGIDSERVAQkalekgqidenqynamtnnekallIFGAGISTADKitdisGRGVG 501
Cdd:PRK11360  518 ARGKIRIRTWQySDGQVAVSIEDNGCGIDPELLKK------------------------IFDPFFTTKAK-----GTGLG 568

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2308515618 502 MDVVKTNIHKLGGVINLDTEIGKGTTITIMLPL 534
Cdd:PRK11360  569 LALSQRIINAHGGDIEVESEPGVGTTFTLYLPI 601
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
544-672 1.97e-05

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 45.25  E-value: 1.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 544 IRVANQKYILPLSSIVESLQPTAdmIKKIgDGTQDLLM----LREEFIPVVKLHQLFGLEKSfEKLEDGMLIVVKSGNTK 619
Cdd:COG0835    13 FRLGGERYAIPIEKVREILPLPP--ITPV-PGAPPWVLgvinLRGRVVPVIDLRALLGLPPT-EDTERTRIIVLEVGGRV 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2308515618 620 VALSIDEFLNQHQV---VVKPLDKNFRS-----VQGIgaatVKGDGSIGLILDVVGIINAQ 672
Cdd:COG0835    89 VGLLVDSVSGVVRIdpdDIEPPPELLSGglapfITGV----AKLDDRLILLLDLEKLLAEE 145
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
401-535 2.00e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 47.71  E-value: 2.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 401 IIRNSLDHGIEmpedrvalGKIETGSISISAEQANGQMIITIQDDGKGIDSERVaqkalekgqidENQYNAMTNNEKall 480
Cdd:COG2972   344 LVENAIEHGIE--------PKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKL-----------EKLLEELSSKGE--- 401

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2308515618 481 ifgagistadkitdisGRGVGMDVVKTNIHKL---GGVINLDTEIGKGTTITIMLPLT 535
Cdd:COG2972   402 ----------------GRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPLE 443
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 404-534 7.27e-05

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: 45.74  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 404 NSLDHGIE-MPEDrvalgkietGSISISA-EQANGQMIITIQDDGKGIDSERvaqkaLEKgqidenqynamtnnekallI 481
Cdd:COG5809   386 NLLKNAIEaMPEG---------GNITIETkAEDDDKVVISVTDEGCGIPEER-----LKK-------------------L 432

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 482 FGAGISTADKitdisGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLPL 534
Cdd:COG5809   433 GEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPI 480
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 353-451 1.51e-04

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


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 42.02  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 353 MDSIYSKFPKVVRDISKKLNKKVEFKHYGDNVEIDKAMIEGLTdpLMHIIRNSLDHGIEmpeDRvalgkiETGSISISAE 432
Cdd:cd16951     1 LGEYINRIASAINAIHAVGDIRINITGDTGPVSSEVATAIGLV--VNELLQNALKHAFS---DR------EGGTITIRSV 69

                          90
                  ....*....|....*....
gi 2308515618 433 QANGQMIITIQDDGKGIDS 451
Cdd:cd16951    70 VDGDYLRITVIDDGVGLPQ 88
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 398-533 1.83e-04

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 41.16  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 398 LMHIIRNSLDHGIEMPEDRvalgkiETGSISISAEQANGQMIITIQDDGKGIDSERvaqkalekgqidenqynamtnNEK 477
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRPR------RPPRIEVGAEDVGEEWTFYVRDNGIGIDPEY---------------------AEK 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2308515618 478 ALLIFgagiSTADKITDISGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:cd16921    54 VFGIF----QRLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
 538-672 1.87e-04

CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. CheW interacts with the histidine kinase CheA, most likely with the related regulatory domain of CheA. CheW is proposed to form signalling arrays together with CheA and the methyl-accepting chemotaxis proteins (MCPs), which are involved in response modulation.


Pssm-ID: 238374  Cd Length: 140  Bit Score: 42.17  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 538 ILDGLDIRVANQKYILPLSSIVESLQPTAdmIKKIgDGTQDLLM----LREEFIPVVKLHQLFGLEkSFEKLEDGMLIVV 613
Cdd:cd00732     1 ELEVVTFRLGDEEYGIPIMQVREILKPTP--ITPI-PNAPPYVLgvinLRGRIVPVIDLRKRLGLP-PAEDTKNTRIIVV 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2308515618 614 KSGNTKVALSIDEFLNQHQVVVKPLDKNFRSVQGIGAATVKG----DGSIGLILDVVGIINAQ 672
Cdd:cd00732    77 EVGDQVVGLLVDSVSEVLRLSTDDIQPPPPVLSDINAKFIRGvvklEGRLLILLDLDKILDER 139
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 425-533 1.24e-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: 38.58  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 425 GSISISAEQANGQMIITIQDDGKGIDSErvaqkalekgQIDEnQYNAMTNNEKAllifgagistadkiTDISGRGVGMDV 504
Cdd:cd16950    18 GWVEVSSDGEGNRTRIQVLDNGPGIAPE----------EVDE-LFQPFYRGDNA--------------RGTSGTGLGLAI 72

                          90       100
                  ....*....|....*....|....*....
gi 2308515618 505 VKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGGLCARIELP 101
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 496-533 1.34e-03

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: 38.90  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2308515618 496 SGRGVGMDVVKTNIHKLGGVINLDTEIGKGTTITIMLP 533
Cdd:cd16919    79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_YpdA-YehU-LytS-like cd16924
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 401-496 2.09e-03

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: 38.20  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308515618 401 IIRNSLDHGIEMPEDrvalgkieTGSISISAEQANGQMIITIQDDGKGIDServaqKALEKGQIDENQYN--AMTN-NEK 477
Cdd:cd16924     9 LVENAIQHGLSPLTD--------KGVVTISALKEDNHVMIEVEDNGRGIDP-----KVLNILGKKPKEGNgiGLYNvHQR 75

                          90       100
                  ....*....|....*....|....
gi 2308515618 478 ALLIFG--AGI---STADKITDIS 496
Cdd:cd16924    76 LILLFGedYGIhiaSEPDKGTRIT 99
 
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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