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Conserved domains on  [gi|503020500|ref|WP_013255476|]
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chemotaxis protein CheA [Sediminispirochaeta smaragdinae]

Protein Classification

chemotaxis protein CheA( domain architecture ID 12188521)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
276-852 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 602.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 276 PEMVQKFVEESSDLLDTAENAALSLERGKETKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGVLDALRKGDRKVDS 355
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 356 KVVNLLLEGIDNLRTSLKQIQSGDlkpgvdtehhiiaekamnsKNAGDYQPLGDLLVEMGVASRESVDEALELQQmrlge 435
Cdd:COG0643   84 ELIDLLLEALDALRALLDALEAGG-------------------EPPADISALLARLDASEEAIEEVVADEVEISP----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 436 ilvkqgkAEPKAVEKALESQGKPAGKNDQFANYRLKRKDIRVDTERLDTLFDLMGELITAEAMVLNSP-ELEEFDHPNFD 514
Cdd:COG0643  140 -------PAPAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAeELEDESLRELE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 515 RSAAYLSKISRELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDH 594
Cdd:COG0643  213 EALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDH 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 595 GIEDPESRKKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAMERGLVQDDQV--LSDKEVFQLIFEPGFST 672
Cdd:COG0643  293 GIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAaaLSDEELLELIFAPGFST 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 673 AEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLAIIDAINFTVGRQLYAIPITDVIQFYKaVGSE 752
Cdd:COG0643  373 AEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR-LDPD 451

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 753 LTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSGNHTAALLADEIVGYRQMVIKALPSYLGNLRAVS 832
Cdd:COG0643  452 DIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGIS 531

                        570       580
                 ....*....|....*....|
gi 503020500 833 GCSIMSDGKVSLIVDTGALL 852
Cdd:COG0643  532 GATILGDGRVALILDVAALV 551
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 109-194 1.30e-20

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: 86.92  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   109 FLQEAREHLDTIEEDILTLEREWSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGTITVDSDCIDILL 188
Cdd:smart00073   6 FREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDLLL 85


                   ....*.
gi 503020500   189 QGSDRL 194
Cdd:smart00073  86 ELVDVL 91
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
276-852 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 602.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 276 PEMVQKFVEESSDLLDTAENAALSLERGKETKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGVLDALRKGDRKVDS 355
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 356 KVVNLLLEGIDNLRTSLKQIQSGDlkpgvdtehhiiaekamnsKNAGDYQPLGDLLVEMGVASRESVDEALELQQmrlge 435
Cdd:COG0643   84 ELIDLLLEALDALRALLDALEAGG-------------------EPPADISALLARLDASEEAIEEVVADEVEISP----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 436 ilvkqgkAEPKAVEKALESQGKPAGKNDQFANYRLKRKDIRVDTERLDTLFDLMGELITAEAMVLNSP-ELEEFDHPNFD 514
Cdd:COG0643  140 -------PAPAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAeELEDESLRELE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 515 RSAAYLSKISRELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDH 594
Cdd:COG0643  213 EALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDH 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 595 GIEDPESRKKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAMERGLVQDDQV--LSDKEVFQLIFEPGFST 672
Cdd:COG0643  293 GIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAaaLSDEELLELIFAPGFST 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 673 AEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLAIIDAINFTVGRQLYAIPITDVIQFYKaVGSE 752
Cdd:COG0643  373 AEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR-LDPD 451

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 753 LTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSGNHTAALLADEIVGYRQMVIKALPSYLGNLRAVS 832
Cdd:COG0643  452 DIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGIS 531

                        570       580
                 ....*....|....*....|
gi 503020500 833 GCSIMSDGKVSLIVDTGALL 852
Cdd:COG0643  532 GATILGDGRVALILDVAALV 551
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 108-851 1.79e-116

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 369.06  E-value: 1.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 108 SFLQEAREHLDTIEEDILTLEREW--SEDLvHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGTITVDSDCID 185
Cdd:PRK10547   9 TFFDEADELLADMEQHLLVLDPEApdAEQL-NAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIIN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 186 ILLQGSDRLNgligslelqaagfhsdkggtvyesgadiddiiDKLDAiLKTnghsdtaasrapapspekerkivehkapA 265
Cdd:PRK10547  88 LFLETKDIMQ--------------------------------EQLDA-YKT----------------------------S 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 266 YDPYADGL--ITPEMVQkfveessdlldtaenaaLSLERGKETKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGvl 343
Cdd:PRK10547 107 QEPDAASFeyICQALRQ-----------------LALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSGLRIILSR-- 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 344 daLRKGDrkvdskvVNLLLEGIDNLRTsLKQIQSGD--LKPGVDT---EHHIIA-------EKAMNSKNAGDYQPlgdll 411
Cdd:PRK10547 168 --LKAGE-------VDLLEEELGNLGT-LTDVVKGAdsLEATLPGsvaEDDITAvlcfvieADQITFETAVAAPQ----- 232

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 412 vemgvASRESVDEALELQQMRLGEILVKQGKAEPKAvekALESQGKPAGKNDQfanyrlkrKDIRVDTERLDTLFDLMGE 491
Cdd:PRK10547 233 -----EKAEETTEVVEVSPKISVPPVLKLAAEQAPA---GRVEREKTARSSES--------TSIRVAVEKVDQLINLVGE 296

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 492 LITAEAMVLN-SPELEEFDHPNFDRSAAYLSKISRELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEET 570
Cdd:PRK10547 297 LVITQSMLAQrSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSST 376

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 571 EMDRNVMEEISDPLVHIIRNAIDHGIEDPESRKKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAMERGLV 650
Cdd:PRK10547 377 ELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLA 456

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 651 QDDQvLSDKEVFQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLAIIDAINFTV 730
Cdd:PRK10547 457 VSEN-MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRV 535

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 731 GRQLYAIPITDVIQFYKAVGSELTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSGNHTAALLADEI 810
Cdd:PRK10547 536 ADEVFILPLNAVMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQL 615

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....
gi 503020500 811 VGYRQMVIKALPSylgNLRAVSGCS---IMSDGKVSLIVDTGAL 851
Cdd:PRK10547 616 IGQHQVVVKNLES---NYRKVPGISaatILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 542-717 9.55e-88

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: 276.00  E-value: 9.55e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 542 LFNKMRRLVRDLSKKFNKEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDHGIEDPESRKKAGKAEDGTIELRARYEG 621
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 622 NEIWVTIADDGGGLNKKRILERAMERGLVQDDQV--LSDKEVFQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGK 699
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAatLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 503020500 700 IDIESQEEKGTTFTLKIP 717
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 582-719 3.07e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 100.80  E-value: 3.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   582 DPLVHIIRNAIDHGIEDPEsrkkagkaEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEV 661
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTP--------EGGRITVTLERDGDHVEITVEDNGPGI----------------------PPED 53

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 503020500   662 FQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:smart00387  54 LEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 109-194 1.30e-20

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: 86.92  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   109 FLQEAREHLDTIEEDILTLEREWSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGTITVDSDCIDILL 188
Cdd:smart00073   6 FREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDLLL 85


                   ....*.
gi 503020500   189 QGSDRL 194
Cdd:smart00073  86 ELVDVL 91
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 102-198 3.89e-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: 82.81  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 102 DPDILFSFLQEAREHLDTIEEDILTLErewSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGtITVDS 181
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELE---DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVTP 76

                         90
                 ....*....|....*..
gi 503020500 182 DCIDILLQGSDRLNGLI 198
Cdd:cd00088   77 ELIDLLLDALDALKAEL 93
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 728-851 1.74e-18

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: 82.25  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  728 FTVGRQLYAIPITDVIQFYKAvgSELTETEE----HRQIITLRGQVLPLIKMKEFFAVtEGKEKAEEGIVIVVRSGNHTA 803
Cdd:pfam01584   4 FRLGGETFAIPISKVREILRP--PPITPIPGapgyVLGVINLRGEVLPVIDLRRLLGL-PPTEPRERTRVVVVEVGGQVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503020500  804 ALLADEIVGYRQMVIKALPSYLGNLRA---VSGCSIMSDGKVSLIVDTGAL 851
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 104-194 7.76e-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: 61.98  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  104 DILFSFLQEAREHLDTieediltLEREWSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLldeLRVGTITVDSDC 183
Cdd:pfam01627   1 ELLELFLEEAPELLEQ-------LEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDPEL 70

                          90
                  ....*....|.
gi 503020500  184 IDILLQGSDRL 194
Cdd:pfam01627  71 LEALRDLLEAL 81
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
276-852 0e+00

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 602.94  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 276 PEMVQKFVEESSDLLDTAENAALSLERGKETKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGVLDALRKGDRKVDS 355
Cdd:COG0643    4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPELLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 356 KVVNLLLEGIDNLRTSLKQIQSGDlkpgvdtehhiiaekamnsKNAGDYQPLGDLLVEMGVASRESVDEALELQQmrlge 435
Cdd:COG0643   84 ELIDLLLEALDALRALLDALEAGG-------------------EPPADISALLARLDASEEAIEEVVADEVEISP----- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 436 ilvkqgkAEPKAVEKALESQGKPAGKNDQFANYRLKRKDIRVDTERLDTLFDLMGELITAEAMVLNSP-ELEEFDHPNFD 514
Cdd:COG0643  140 -------PAPAALEPAPAAAPPAEAAAAAAEAAAAASETVRVDVERLDRLMNLVGELVITRARLEQLAeELEDESLRELE 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 515 RSAAYLSKISRELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDH 594
Cdd:COG0643  213 EALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRDLARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDH 292

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 595 GIEDPESRKKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAMERGLVQDDQV--LSDKEVFQLIFEPGFST 672
Cdd:COG0643  293 GIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAKAIEKGLITAEEAaaLSDEELLELIFAPGFST 372

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 673 AEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLAIIDAINFTVGRQLYAIPITDVIQFYKaVGSE 752
Cdd:COG0643  373 AEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLR-LDPD 451

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 753 LTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSGNHTAALLADEIVGYRQMVIKALPSYLGNLRAVS 832
Cdd:COG0643  452 DIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERGPVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGIS 531

                        570       580
                 ....*....|....*....|
gi 503020500 833 GCSIMSDGKVSLIVDTGALL 852
Cdd:COG0643  532 GATILGDGRVALILDVAALV 551
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
 108-851 1.79e-116

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 369.06  E-value: 1.79e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 108 SFLQEAREHLDTIEEDILTLEREW--SEDLvHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGTITVDSDCID 185
Cdd:PRK10547   9 TFFDEADELLADMEQHLLVLDPEApdAEQL-NAIFRAAHSIKGGAGTFGFTVLQETTHLMENLLDEARRGEMQLNTDIIN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 186 ILLQGSDRLNgligslelqaagfhsdkggtvyesgadiddiiDKLDAiLKTnghsdtaasrapapspekerkivehkapA 265
Cdd:PRK10547  88 LFLETKDIMQ--------------------------------EQLDA-YKT----------------------------S 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 266 YDPYADGL--ITPEMVQkfveessdlldtaenaaLSLERGKETKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGvl 343
Cdd:PRK10547 107 QEPDAASFeyICQALRQ-----------------LALEAKGETPSAVTRLSVVAIQEKSEPQDESPRSQSGLRIILSR-- 167

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 344 daLRKGDrkvdskvVNLLLEGIDNLRTsLKQIQSGD--LKPGVDT---EHHIIA-------EKAMNSKNAGDYQPlgdll 411
Cdd:PRK10547 168 --LKAGE-------VDLLEEELGNLGT-LTDVVKGAdsLEATLPGsvaEDDITAvlcfvieADQITFETAVAAPQ----- 232

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 412 vemgvASRESVDEALELQQMRLGEILVKQGKAEPKAvekALESQGKPAGKNDQfanyrlkrKDIRVDTERLDTLFDLMGE 491
Cdd:PRK10547 233 -----EKAEETTEVVEVSPKISVPPVLKLAAEQAPA---GRVEREKTARSSES--------TSIRVAVEKVDQLINLVGE 296

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 492 LITAEAMVLN-SPELEEFDHPNFDRSAAYLSKISRELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEET 570
Cdd:PRK10547 297 LVITQSMLAQrSSELDPVNHGDLITSMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSST 376

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 571 EMDRNVMEEISDPLVHIIRNAIDHGIEDPESRKKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAMERGLV 650
Cdd:PRK10547 377 ELDKSLIERIIDPLTHLVRNSLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQGLA 456

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 651 QDDQvLSDKEVFQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLAIIDAINFTV 730
Cdd:PRK10547 457 VSEN-MSDEEVGMLIFAPGFSTAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSKQGKGTTIRILLPLTLAILDGMSVRV 535

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 731 GRQLYAIPITDVIQFYKAVGSELTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSGNHTAALLADEI 810
Cdd:PRK10547 536 ADEVFILPLNAVMESLQPREEDLHPLAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQL 615

                        730       740       750       760
                 ....*....|....*....|....*....|....*....|....
gi 503020500 811 VGYRQMVIKALPSylgNLRAVSGCS---IMSDGKVSLIVDTGAL 851
Cdd:PRK10547 616 IGQHQVVVKNLES---NYRKVPGISaatILGDGSVALIVDVSAL 656
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
 542-717 9.55e-88

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: 276.00  E-value: 9.55e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 542 LFNKMRRLVRDLSKKFNKEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDHGIEDPESRKKAGKAEDGTIELRARYEG 621
Cdd:cd16916    1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 622 NEIWVTIADDGGGLNKKRILERAMERGLVQDDQV--LSDKEVFQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGK 699
Cdd:cd16916   81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAatLSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160

                        170
                 ....*....|....*...
gi 503020500 700 IDIESQEEKGTTFTLKIP 717
Cdd:cd16916  161 IEVESEPGQGTTFTIRLP 178
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
 720-851 4.18e-28

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: 109.96  E-value: 4.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 720 LAIIDAINFTVGRQLYAIPITDVIQFYKAVGSELTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSG 799
Cdd:cd00731    1 LAIIKGLLVRVGDETYAIPLSAVVETVRIKPKDIKRVDGGKEVINVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503020500 800 NHTAALLADEIVGYRQMVIKALPSYLGNLRAVSGCSIMSDGKVSLIVDTGAL 851
Cdd:cd00731   81 GRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVALILDVPAL 132
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 582-719 3.07e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 100.80  E-value: 3.07e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   582 DPLVHIIRNAIDHGIEDPEsrkkagkaEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEV 661
Cdd:smart00387   4 DRLRQVLSNLLDNAIKYTP--------EGGRITVTLERDGDHVEITVEDNGPGI----------------------PPED 53

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 503020500   662 FQLIFEPGFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:smart00387  54 LEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 109-194 1.30e-20

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: 86.92  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   109 FLQEAREHLDTIEEDILTLEREWSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGTITVDSDCIDILL 188
Cdd:smart00073   6 FREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPDLLDLLL 85


                   ....*.
gi 503020500   189 QGSDRL 194
Cdd:smart00073  86 ELVDVL 91
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 102-198 3.89e-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: 82.81  E-value: 3.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 102 DPDILFSFLQEAREHLDTIEEDILTLErewSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLLDELRVGtITVDS 181
Cdd:cd00088    1 MEELLELFLEEAEELLEELERALLELE---DAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVTP 76

                         90
                 ....*....|....*..
gi 503020500 182 DCIDILLQGSDRLNGLI 198
Cdd:cd00088   77 ELIDLLLDALDALKAEL 93
CheW smart00260
Two component signalling adaptor domain;
713-852 6.91e-19

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 83.83  E-value: 6.91e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   713 TLKIPLTLAIIDainftvgRQLYAIPITDVIQFYKAvgSELTETEEHRQ----IITLRGQVLPLIKMKEFFAVTEGKEKa 788
Cdd:smart00260   1 TIRLPLTFAIGK-------DETYAIPIAAVREILRP--PPITPIPGAPGyvlgVINLRGEVLPVVDLRRLLGLPPEPPT- 70

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503020500   789 EEGIVIVVRSGNHTAALLADEIVGYRQMVIKAL----PSYLGNLRAVSGCSIMSDGKVSLIVDTGALL 852
Cdd:smart00260  71 DETRVIVVETGDRKVGLVVDSVLGVREVVVKSIepppPVSLSNAPGISGATILGDGRVVLILDVDKLL 138
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
 728-851 1.74e-18

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: 82.25  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  728 FTVGRQLYAIPITDVIQFYKAvgSELTETEE----HRQIITLRGQVLPLIKMKEFFAVtEGKEKAEEGIVIVVRSGNHTA 803
Cdd:pfam01584   4 FRLGGETFAIPISKVREILRP--PPITPIPGapgyVLGVINLRGEVLPVIDLRRLLGL-PPTEPRERTRVVVVEVGGQVV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503020500  804 ALLADEIVGYRQMVIKALPSYLGNLRA---VSGCSIMSDGKVSLIVDTGAL 851
Cdd:pfam01584  81 GLLVDEVIGVLEIVIKQIEPPLGLGRVagyISGATILGDGRVVLILDVEAL 131
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
520-719 3.66e-18

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 84.57  E-value: 3.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 520 LSKIsrELQEITMTIRMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEETE--MDRNVMEEIsdpLVHIIRNAIDHGie 597
Cdd:COG2205   76 LSRL--ESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLvyADPELLEQV---LANLLDNAIKYS-- 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 598 dpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQLIFEPgFSTAEQVS 677
Cdd:COG2205  149 ----------PPGGTITISARREGDGVRISVSDNGPGI----------------------PEEELERIFER-FYRGDNSR 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 503020500 678 EISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG2205  196 GEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLA 237
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
 722-851 1.88e-17

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: 79.63  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 722 IIDAINFTVGRQLYAIPITDV--IQFYKAVGSELTETEEHRQIITLRGQVLPLIKMKEFFAVTEGKEKAEEGIVIVVRSG 799
Cdd:cd00588    1 ILQVLLFRVGDELYAIPIAVVeeILPLPPITRVPNAPDYVLGVINLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503020500 800 NHTAALLADEIVGYRQMVIKAL----PSYLGNLRAVSGCSIMSDGKVSLIVDTGAL 851
Cdd:cd00588   81 DRKVGLVVDSVLGVLEVVIKDIepppDVGSSNAPGISGATILGDGRVVLILDVDKL 136
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
514-719 3.38e-17

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 83.80  E-value: 3.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 514 DRSAAYLSKISRELQEIT------MTIRMIPMDglfnkMRRLVRDLSKKF-----NKEISLVVSGEET----EMDRNVME 578
Cdd:COG0642  151 LRSADRLLRLINDLLDLSrleagkLELEPEPVD-----LAELLEEVVELFrplaeEKGIELELDLPDDlptvRGDPDRLR 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 579 EIsdpLVHIIRNAIDHGiedpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsD 658
Cdd:COG0642  226 QV---LLNLLSNAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPGI----------------------P 268

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503020500 659 KEVFQLIFEPgFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG0642  269 PEDLERIFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 581-719 6.33e-17

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: 77.02  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  581 SDPLVHIIRNAIDHGIedpesrKKAGKAEDGTIELRaryEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKE 660
Cdd:pfam02518   3 ELRLRQVLSNLLDNAL------KHAAKAGEITVTLS---EGGELTLTVEDNGIGI----------------------PPE 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 503020500  661 VFQLIFEPgFSTAEQVSeISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:pfam02518  52 DLPRIFEP-FSTADKRG-GGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 514-721 8.55e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 80.28  E-value: 8.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 514 DRSAAYLSKISRELQEITMT----IRMIPMDGLFNKMRRLVRDlskkfnKEISLVVSgEETEMDRNVMEEISdpLVHIIR 589
Cdd:COG3290  217 DEALEYIDEISEELQELIDSllsrIGNPVLAALLLGKAARARE------RGIDLTID-IDSDLPDLPLSDTD--LVTILG 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 590 NAIDHGIEDPEsrkkAGKAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQLIFEPG 669
Cdd:COG3290  288 NLLDNAIEAVE----KLPEEERRVELSIRDDGDELVIEVEDSGPGI----------------------PEELLEKIFERG 341

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503020500 670 FSTAEQvseiSGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLTLA 721
Cdd:COG3290  342 FSTKLG----EGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEGE 389
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 509-719 5.80e-14

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 74.45  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 509 DHPNFDRSAAYLSKISRELQEITMTIR--------------MIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGE--ETEM 572
Cdd:COG4191  173 DEPDPEELREALERILEGAERAAEIVRslrafsrrdeeerePVDLNELIDEALELLRPRLKARGIEVELDLPPDlpPVLG 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 573 DRNVMEEIsdpLVHIIRNAIDhGIEDpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqd 652
Cdd:COG4191  253 DPGQLEQV---LLNLLINAID-AMEE---------GEGGRITISTRREGDYVVISVRDNGPGI----------------- 302

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503020500 653 dqvlsDKEVFQLIFEPGFSTAEqvsEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG4191  303 -----PPEVLERIFEPFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 535-719 7.20e-14

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: 74.61  E-value: 7.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 535 RMIPMDGLFNKMRRLVRDLSKKFNKEISLVVSGEETE--MDRNVMEEIsdpLVHIIRNAIDHGiedpesrkkagkAEDGT 612
Cdd:COG5000  274 EPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEvlADRDQLEQV---LINLLKNAIEAI------------EEGGE 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 613 IELRARYEGNEIWVTIADDGGGLNKKrILERamerglvqddqvlsdkevfqlIFEPGFSTAEqvseiSGRGVGMDVVKKN 692
Cdd:COG5000  339 IEVSTRREDGRVRIEVSDNGPGIPEE-VLER---------------------IFEPFFTTKP-----KGTGLGLAIVKKI 391

                        170       180
                 ....*....|....*....|....*..
gi 503020500 693 LEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG5000  392 VEEHGGTIELESRPGGGTTFTIRLPLA 418
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
 561-717 9.71e-14

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 74.95  E-value: 9.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 561 ISLVVSgEETEMDRNVMEEISDPLVHIIRNAIDHGIEdpesrkKAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRI 640
Cdd:PRK11086 412 ITLIIS-EDSQLPDSGDEDQVHELITILGNLIENALE------AVGGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEI 484

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503020500 641 leramerglvqddqvlsdkevfQLIFEPGFSTAEqvseiSGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:PRK11086 485 ----------------------DAIFDKGYSTKG-----SNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
520-718 1.43e-13

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 73.43  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 520 LSKIsrELQEITMTIRMIPMDGLFNKMRRLVRDLSKKfnKEISLVVSGEET----EMDRNVMEEIsdpLVHIIRNAIDHG 595
Cdd:COG5002  225 LSRL--ESGELKLEKEPVDLAELLEEVVEELRPLAEE--KGIELELDLPEDpllvLGDPDRLEQV---LTNLLDNAIKYT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 596 iedpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGlnkkrILERAMERglvqddqvlsdkevfqlIFEPgFSTAEQ 675
Cdd:COG5002  298 ------------PEGGTITVSLREEDDQVRISVRDTGIG-----IPEEDLPR-----------------IFER-FYRVDK 342

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 503020500 676 V--SEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:COG5002  343 SrsRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPL 387
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
 277-373 1.91e-13

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: 66.64  E-value: 1.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 277 EMVQKFVEESSDLLDTAENAALSLERGKetkaNIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGVLDALRKGdRKVDSK 356
Cdd:cd00088    3 ELLELFLEEAEELLEELERALLELEDAE----DLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDG-LEVTPE 77

                         90
                 ....*....|....*..
gi 503020500 357 VVNLLLEGIDNLRTSLK 373
Cdd:cd00088   78 LIDLLLDALDALKAELE 94
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
 277-369 2.10e-13

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: 66.50  E-value: 2.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500   277 EMVQKFVEESSDLLDTAENAALSLERGKETKaNIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEGVLDALRKGDRKVDSK 356
Cdd:smart00073   1 GGLELFREELAEFLQSLEEGLLELEKALDAQ-DVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGEVELTPD 79

                           90
                   ....*....|...
gi 503020500   357 VVNLLLEGIDNLR 369
Cdd:smart00073  80 LLDLLLELVDVLK 92
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 104-194 7.76e-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: 61.98  E-value: 7.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  104 DILFSFLQEAREHLDTieediltLEREWSEDLVHAIFRSMHTIKGVSGFIGLKKIKQLSHRLENLldeLRVGTITVDSDC 183
Cdd:pfam01627   1 ELLELFLEEAPELLEQ-------LEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDPEL 70

                          90
                  ....*....|.
gi 503020500  184 IDILLQGSDRL 194
Cdd:pfam01627  71 LEALRDLLEAL 81
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 558-719 1.08e-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: 68.22  E-value: 1.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 558 NKEISLVVSGE--ETEMDRNvmeEISDPLVHIIRNAIDhGIEDPesrkkagkaedGTIELRARYEGNEIWVTIADDGGGL 635
Cdd:COG5805  375 NIQIRLELLDEdpFIYCDEN---QIKQVFINLIKNAIE-AMPNG-----------GTITIHTEEEDNSVIIRVIDEGIGI 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 636 nkkrileramerglvqddqvlsDKEVFQLIFEPGFSTAEQvseisGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLK 715
Cdd:COG5805  440 ----------------------PEERLKKLGEPFFTTKEK-----GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492


                 ....
gi 503020500 716 IPLT 719
Cdd:COG5805  493 LPLS 496
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 584-717 3.27e-11

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: 60.76  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 584 LVHIIRNAIDHGIeDPESRKKAGKAEdgtIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQ 663
Cdd:cd16915    1 LITIVGNLIDNAL-DALAATGAPNKQ---VEVFLRDEGDDLVIEVRDTGPGI----------------------APELRD 54

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503020500 664 LIFEPGFSTAEQvseiSGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:cd16915   55 KVFERGVSTKGQ----GERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
 277-369 6.03e-10

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: 56.59  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500  277 EMVQKFVEESSDLLDTAENAAlslergkeTKANIEEAFRVVHTIKGNAGFFWFGTVEGMCMAIEgvlDALRKGDRKVDSK 356
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQAL--------DAEDLEALFRAAHTLKGSAGSLGLPALAELAHELE---DLLREGELPLDPE 69

                          90
                  ....*....|...
gi 503020500  357 VVNLLLEGIDNLR 369
Cdd:pfam01627  70 LLEALRDLLEALR 82
H-kinase_dim pfam02895
Signal transducing histidine kinase, homodimeric domain; This helical bundle domain is the ...
 475-534 8.22e-10

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: 55.32  E-value: 8.22e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503020500  475 IRVDTERLDTLFDLMGELITAEAMVLNSPELEEF-----DHPNFDRSAAYLSKISRELQEITMTI 534
Cdd:pfam02895   2 IRVDVEKLDRLMNLVGELVIARNRLVQLLERLEEyggdtLLEELKEALQQLDRLTRELQEAVMKI 66
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
542-719 1.29e-09

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 61.02  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 542 LFNKMRRLVRDLskkFNKEISLVV----SGEETEMDRnvmEEISDPLVHIIRNAIDHGiedpesrkkagkAEDGTIELRA 617
Cdd:COG3852  209 VLERVLELLRAE---APKNIRIVRdydpSLPEVLGDP---DQLIQVLLNLVRNAAEAM------------PEGGTITIRT 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 618 RYE----------GNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQLIFEPGFSTAEQvseisGRGVGMD 687
Cdd:COG3852  271 RVErqvtlgglrpRLYVRIEVIDNGPGI----------------------PEEILDRIFEPFFTTKEK-----GTGLGLA 323

                        170       180       190
                 ....*....|....*....|....*....|..
gi 503020500 688 VVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG3852  324 IVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
587-719 1.58e-09

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 61.19  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 587 IIRNAIDHGIEDpesrkkagKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRIleramerglvqddqvlsdKEVFQLIF 666
Cdd:COG2972  344 LVENAIEHGIEP--------KEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKL------------------EKLLEELS 397

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503020500 667 EPGfstaeqvseiSGRGVGMDVVKKNLEKLRGK---IDIESQEEKGTTFTLKIPLT 719
Cdd:COG2972  398 SKG----------EGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLE 443
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
552-718 1.28e-07

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 55.36  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 552 DLSKKFNKEISLVVSgeetemDRNVMEEIsdpLVHIIRNAIDhgiedpesrkkaGKAEDGTIELRARYEGN-EIWVTIAD 630
Cdd:PRK11360 482 DFETELDNELPPIWA------DPELLKQV---LLNILINAVQ------------AISARGKIRIRTWQYSDgQVAVSIED 540

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 631 DGGGLnkkrileramerglvqddqvlsDKEVFQLIFEPGFSTAEQvseisGRGVGMDVVKKNLEKLRGKIDIESQEEKGT 710
Cdd:PRK11360 541 NGCGI----------------------DPELLKKIFDPFFTTKAK-----GTGLGLALSQRIINAHGGDIEVESEPGVGT 593


                 ....*...
gi 503020500 711 TFTLKIPL 718
Cdd:PRK11360 594 TFTLYLPI 601
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
 584-717 2.09e-07

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 54.41  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 584 LVHIIRNAIDHGiedpesrkkaGKAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQ 663
Cdd:COG4251  399 FQNLISNAIKYS----------RPGEPPRIEIGAEREGGEWVFSVRDNGIGI----------------------DPEYAE 446

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503020500 664 LIFEPgFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:COG4251  447 KIFEI-FQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
CheW COG0835
Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];
728-852 2.18e-07

Chemotaxis signal transduction protein CheW [Signal transduction mechanisms];


Pssm-ID: 440597  Cd Length: 151  Bit Score: 51.03  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 728 FTVGRQLYAIPITDViqfykavgSELTETEEHRQI----------ITLRGQVLPLIKMKEFFAVTEgKEKAEEGIVIVVR 797
Cdd:COG0835   13 FRLGGERYAIPIEKV--------REILPLPPITPVpgappwvlgvINLRGRVVPVIDLRALLGLPP-TEDTERTRIIVLE 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 798 SGNHTAALLADEIVG---YRQMVIKALPSYLGNLRA--VSGCsIMSDGKVSLIVDTGALL 852
Cdd:COG0835   84 VGGRVVGLLVDSVSGvvrIDPDDIEPPPELLSGGLApfITGV-AKLDDRLILLLDLEKLL 142
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 587-717 2.27e-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: 49.74  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 587 IIRNAIDHGIEdpesrkkaGKAEDGTIELRARYEGNEIWVTIADDGGGLN---KKRILERamerglvqddqvlsdkevfq 663
Cdd:cd16956    9 IVENAVKHGLS--------GLLDGGRVEITARLDGQHLLLEVEDNGGGMDpdtLARILIR-------------------- 60

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503020500 664 lifepgfstaeqvseiSGRGVGMDVVKKNLEKLRGK---IDIESQEEKGTTFTLKIP 717
Cdd:cd16956   61 ----------------SSNGLGLNLVDKRLRQAFGNdygLDIECAPGEGTRITIRLP 101
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 584-718 2.84e-07

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 53.83  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 584 LVHIIRNAIdhgiedpESRKKAGKAedgTIELRArYEGNEIWVTIADDGGGLNKKRIleramerglvqddqvlsdkevfQ 663
Cdd:COG5809  384 FINLLKNAI-------EAMPEGGNI---TIETKA-EDDDKVVISVTDEGCGIPEERL----------------------K 430

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503020500 664 LIFEPGFSTAEQvseisGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:COG5809  431 KLGEPFYTTKEK-----GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPI 480
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 608-717 5.98e-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: 48.82  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 608 AEDGTIELRARYEGNEIWVTIADDGGGLNKKRILEramerglvqddqvlsdkevfqlIFEPGFSTAEQVSEISGRGVGMD 687
Cdd:cd16948   22 KQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPR----------------------VFDKGFTGENGRNFQESTGMGLY 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 503020500 688 VVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:cd16948   80 LVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
CheW cd00732
CheW, a small regulator protein, unique to the chemotaxis signalling in prokaryotes and archea. ...
 726-810 1.26e-06

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: 48.72  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 726 INFTVGRQLYAIPITDVIQFYKAVG-SELTETEEH-RQIITLRGQVLPLIKMKEFFAVTEgKEKAEEGIVIVVRSGNHTA 803
Cdd:cd00732    5 VTFRLGDEEYGIPIMQVREILKPTPiTPIPNAPPYvLGVINLRGRIVPVIDLRKRLGLPP-AEDTKNTRIIVVEVGDQVV 83


                 ....*..
gi 503020500 804 ALLADEI 810
Cdd:cd00732   84 GLLVDSV 90
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
 609-718 2.60e-06

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: 46.72  E-value: 2.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 609 EDGTIELRARYEGNE-----IWVTIADDGGGLNkkrileramerglvQDDQvlsdkevfQLIFEPgFSTAEqvSEISGR- 682
Cdd:cd16922   17 EEGEVTLRVSLEEEEedgvqLRFSVEDTGIGIP--------------EEQQ--------ARLFEP-FSQAD--SSTTRKy 71

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 503020500 683 ---GVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:cd16922   72 ggtGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 578-718 4.41e-06

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: 46.26  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 578 EEISDPLVHIIRNAIdHGIEdpesrkkagkaEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvls 657
Cdd:cd16943    2 SQLNQVLLNLLVNAA-QAME-----------GRGRITIRTWAHVDQVLIEVEDTGSGI---------------------- 47

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503020500 658 DKEVFQLIFEPgFSTAEQVSEisGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:cd16943   48 DPEILGRIFDP-FFTTKPVGE--GTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILPI 105
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
497-719 5.81e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 48.46  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 497 AMVLNSPELEEFDHPNFDRSAAYLSKISRELQEITMTIR---------MIPMDGLFNKMRRLVRDLSKKFNKEISLVVSG 567
Cdd:COG4585   71 AIKLQLEAARRLLDADPEAAREELEEIRELAREALAELRrlvrglrppALDDLGLAAALEELAERLLRAAGIRVELDVDG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 568 EETEMDrnvmEEISDPLVHIIR----NAIDHgiedpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGLNkkriler 643
Cdd:COG4585  151 DPDRLP----PEVELALYRIVQealtNALKH-------------AGATRVTVTLEVDDGELTLTVRDDGVGFD------- 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503020500 644 amerglvqddqvlsdkevfqlifepgfstaeqVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:COG4585  207 --------------------------------PEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 584-714 7.06e-06

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 45.53  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 584 LVHIIRNAIDhgiedpesrkKAGKAEDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQ 663
Cdd:cd16976    5 LMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI----------------------AEEHLS 52

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503020500 664 LIFEPGFSTAEqVSEisGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTL 714
Cdd:cd16976   53 RVFDPFFTTKP-VGK--GTGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 650-717 3.27e-05

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: 43.47  E-value: 3.27e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503020500 650 VQDDQVLSDKEVFQLIFEPgFSTAEQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:cd16921   39 VRDNGIGIDPEYAEKVFGI-FQRLHSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
609-718 3.93e-05

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 47.09  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 609 EDGTIELRARYEGNEIWVTIADDGGGlnkkrILERAMERglvqddqvlsdkevfqlIFEPGFSTAEQvseisGRGVGMDV 688
Cdd:PRK10364 366 QHGVISVTASESGAGVKISVTDSGKG-----IAADQLEA-----------------IFTPYFTTKAE-----GTGLGLAV 418

                         90       100       110
                 ....*....|....*....|....*....|
gi 503020500 689 VKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:PRK10364 419 VHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
 546-719 1.06e-04

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 45.67  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 546 MRRLVRDLSKKF-----NKEISLVVSGEETEMDrnvmEEISDPL---VH-IIRNAIDHGiedpesrkkAGKAEDGTIELR 616
Cdd:COG3920  361 LRDYLRELLEPLrdsygGRGIRIELDGPDVELP----ADAAVPLgliLNeLVTNALKHA---------FLSGEGGRIRVS 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 617 ARYEGNEIWVTIADDGGGLNkkrileramerglvqddqvlsdkevfqlifepgfstaEQVSEISGRGVGMDVVKKNLEKL 696
Cdd:COG3920  428 WRREDGRLRLTVSDNGVGLP-------------------------------------EDVDPPARKGLGLRLIRALVRQL 470

                        170       180
                 ....*....|....*....|...
gi 503020500 697 RGKIDIESqeEKGTTFTLKIPLT 719
Cdd:COG3920  471 GGTLELDR--PEGTRVRITFPLA 491
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
 620-717 1.18e-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: 42.37  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 620 EGNEIWVTIADDGGGLnkkrileramerglvqddqvlsDKEVFQLIFEPGFSTAEqvsEISGRGVGMDVVKKNLEKLRGK 699
Cdd:cd16919   44 PGNYVCLEVSDTGSGM----------------------PAEVLRRAFEPFFTTKE---VGKGTGLGLSMVYGFVKQSGGH 98

                         90
                 ....*....|....*...
gi 503020500 700 IDIESQEEKGTTFTLKIP 717
Cdd:cd16919   99 LRIYSEPGVGTTVRIYLP 116
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 587-718 1.72e-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: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 587 IIRNAIDHGiedpesrkkagkaeDGTIELRARYEGNEIWVTIADDGGGlnkkrileramerglVQDDQVLSdkevfqlIF 666
Cdd:cd16949    8 VLRNALRYS--------------PSKILLDISQDGDQWTITITDDGPG---------------VPEDQLEQ-------IF 51

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503020500 667 EPGFSTAEQVS-EISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:cd16949   52 LPFYRVDSARDrESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 580-717 8.04e-04

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 39.83  E-value: 8.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 580 ISDPLVHIIRNAIDhGIEDpesrkkagkAEDGTIELRARYEGN---EIWVTIADDGGGLnkkrileramerglvqddqvl 656
Cdd:cd16944    5 ISQVLTNILKNAAE-AIEG---------RPSDVGEVRIRVEADqdgRIVLIVCDNGKGF--------------------- 53

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503020500 657 sDKEVFQLIFEPGFSTAEQvseisGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:cd16944   54 -PREMRHRATEPYVTTRPK-----GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
nfrB PRK11234
phage adsorption protein NrfB;
405-455 8.86e-04

phage adsorption protein NrfB;


Pssm-ID: 236884 [Multi-domain]  Cd Length: 727  Bit Score: 42.80  E-value: 8.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503020500 405 QPLGDLLVEMGVASRESVDEALE--LQQMRLGEILVKQGKAEPKAVEKALESQ 455
Cdd:PRK11234 482 RPLGQILLENGVITEEQLDTALRnrVRGLRLGQSLLMQGLISAEQLAQALAEQ 534
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
587-649 2.39e-03

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 38.74  E-value: 2.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503020500 587 IIRNAIDHGiedpesrkkAGKAEDGTIELRARYEGNEIWVTIADDGGGLNKKRILERAME-----RGL 649
Cdd:COG2172   42 AVTNAVRHA---------YGGDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYSTlaeggRGL 100
nfrB PRK15489
glycosyl transferase family protein;
405-456 2.66e-03

glycosyl transferase family protein;


Pssm-ID: 237974 [Multi-domain]  Cd Length: 703  Bit Score: 41.27  E-value: 2.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503020500 405 QPLGDLLVEMGVASRESVDEALELQQ---MRLGEILVKQGKAEPKAVEKALESQG 456
Cdd:PRK15489 491 RRLGELLLTWQAVTPEQLQAALAEQQtrgKPLGRILLSQGWLDDETLAEAIAFQA 545
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
650-718 2.92e-03

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 41.50  E-value: 2.92e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503020500 650 VQDDQV-LSDKEVFQLiFEPGFSTAEQV-SEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIPL 718
Cdd:PRK10841 598 VRDTGVgIPAKEVVRL-FDPFFQVGTGVqRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPL 667
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 559-635 4.59e-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: 38.17  E-value: 4.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503020500 559 KEISLVVSGEETEMDRNVMEEISDPLVHIIRNAIDHGIEDpesrkkagkAEDGTIELRARYEGNEIWVTIADDGGGL 635
Cdd:cd16951   19 GDIRINITGDTGPVSSEVATAIGLVVNELLQNALKHAFSD---------REGGTITIRSVVDGDYLRITVIDDGVGL 86
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
 586-717 4.96e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 40.59  E-value: 4.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 586 HIIRNAIDHGIEDPESrkkagkaeDGTIELRARYEGNEIWVTIADDGGGLnkkrileramerglvqdDQVLSDKevfqlI 665
Cdd:PRK15053 439 NLLDNAFEASLRSDEG--------NKIVELFLSDEGDDVVIEVADQGCGV-----------------PESLRDK-----I 488

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503020500 666 FEPGFSTaeQVSEISGRGVGMDVVKKNLEKLRGKIDIESQEEKGTTFTLKIP 717
Cdd:PRK15053 489 FEQGVST--RADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
PRK15347 PRK15347
two component system sensor kinase;
609-719 5.32e-03

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 40.40  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 609 EDGTIELRARYEGNEIWVTIADDGGGLNKKRIleramerglvqddqvlsdkevfQLIFEPGFstaeQVSE-ISGRGVGMD 687
Cdd:PRK15347 530 ETGGIRLRVKRHEQQLCFTVEDTGCGIDIQQQ----------------------QQIFTPFY----QADThSQGTGLGLT 583

                         90       100       110
                 ....*....|....*....|....*....|..
gi 503020500 688 VVKKNLEKLRGKIDIESQEEKGTTFTLKIPLT 719
Cdd:PRK15347 584 IASSLAKMMGGELTLFSTPGVGSCFSLVLPLN 615
EFh_PI-PLC21 cd16213
EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family ...
 426-518 5.72e-03

EF-hand motif found in phosphoinositide phospholipase PLC21 and similar proteins; The family includes invertebrate homologs of phosphoinositide phospholipase C beta (PI-PLC-beta) named PLC21 from cephalopod retina. It also includes PLC21 encoded by plc-21 gene, which is expressed in the central nervous system of Drosophila. Like beta-class of vertebrate PI-PLCs, PLC21 contains an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence.


Pssm-ID: 320043  Cd Length: 154  Bit Score: 38.44  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503020500 426 LELQQMRLGEILVK-------QGKAEPKAVEKALESQGKPAGKND-------------QFANYRLKRKDIrvdterlDTL 485
Cdd:cd16213    7 LTLQTDKEGKIPVKnivkmfaQHKDDRKRVEKALEAIGLPSGKNDaidpkkftfedffNFYRRLTGRQEV-------EKI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 503020500 486 FDLMGE----LITAEAMV--LNS----PELEEFDHPNFDRSAA 518
Cdd:cd16213   80 FDELGAkkkpYLTTEQFVdfLNKtqrdPRLNEILYPYANPKRA 122
 
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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