NCBI Conserved Domain Search

Conserved domains on [gi|1232315758|gb|OYV96811|]

View

MAG: hypothetical protein B7Z73_00130 [Planctomycetia bacterium 21-64-5]

Protein Classification

Graphical summary

Zoom to residue level

show extra options »

Show site features Horizontal zoom: ×

List of domain hits

Name

Accession

Description

Interval

E-value

KdpD

COG2205

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

151-385

4.40e-85

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

Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 264.08 E-value: 4.40e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 151 NSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSG-ALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLR 229
Cdd:COG2205     6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 230 LNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRS 309
Cdd:COG2205    86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARREGDGV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 310 QIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSA 385
Cdd:COG2205   166 RISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVES-EPGGGTTFTVTLPLAE 238

REC_2_DhkD-like

cd17580

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...

416-525

3.56e-44

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 152.23 E-value: 3.56e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeGGRVPAMAL 495
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW--LANTPAIAL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDEL 108

GAF

pfam01590

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...

2-146

1.13e-04

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 42.08 E-value: 1.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758   2 SMEKMLQVITDTAREIIGAHRATAvttWDQNWARCKTTLSLSPEFGPRRPLLSPSSGCELhtlwLALGRAgrLSSAELLA 81
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCAL---YLPDADGLEYLPPGARWLKAAGLEIPPGTGVTV----LRTGRP--LVVPDAAG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758  82 HPAWHTLGPSLCDFGqPPDWLAAPLTgRDGRDMGLLhVCGKCQGDFTSEDEAVLLQLAQMASIAI 146
Cdd:pfam01590  72 DPRFLDPLLLLRNFG-IRSLLAVPII-DDGELLGVL-VLHHPRPPFTEEELELLEVLADQVAIAL 133

Name

Accession

Description

Interval

E-value

KdpD

COG2205

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

151-385

4.40e-85

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

Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 264.08 E-value: 4.40e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 151 NSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSG-ALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLR 229
Cdd:COG2205     6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 230 LNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRS 309
Cdd:COG2205    86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARREGDGV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 310 QIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSA 385
Cdd:COG2205   166 RISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVES-EPGGGTTFTVTLPLAE 238

TMAO_torS

TIGR02956

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...

153-531

9.99e-60

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]

Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 213.49 E-value: 9.99e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 153 EAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTAdEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNV 232
Cdd:TIGR02956 456 EAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTS-QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 233 RPLSLASVIEAALDVVRPAADAKAVRfepLLDERAGHVT----GDPDRLQQVVWNLLVNAVKFSPVGG-KIRVSLTRQGS 307
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQ---LRLNIPEQLPnwwqGDGPRIRQVLINLVGNAIKFTDRGSvVLRVSLNDDSS 611

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 308 RSqIEVADEGEGIDSDIMPHIFDRFRQADSstRRSHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSavv 387
Cdd:TIGR02956 612 LL-FEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESE-LGVGSCFWFTLPLT--- 684

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 388 aegHAQRPDTSAPRAAaprseIDLSGVRVLVVDDEP-DGREAIAKVLSVYHaQVATASSAREALALFAQARPDVLISDIG 466
Cdd:TIGR02956 685 ---RGKPAEDSATLTV-----IDLPPQRVLLVEDNEvNQMVAQGFLTRLGH-KVTLAESGQSALECFHQHAFDLALLDIN 755

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758 467 MPEEDGYDLIRRVRDLAPAEgGRVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:TIGR02956 756 LPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819

PRK15347

two component system sensor kinase;

153-529

2.70e-51

two component system sensor kinase;

Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 189.08 E-value: 2.70e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 153 EAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTAdEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNV 232
Cdd:PRK15347  390 RAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTA-EQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSL 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 233 RPLSLASVIEAALDVVRPAADAKAVRFEPLL-DERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGkIRVSLTRQGSRSQI 311
Cdd:PRK15347  469 EETALLPLLDQAMLTIQGPAQSKSLTLRTFVgAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG-IRLRVKRHEQQLCF 547

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 312 EVADEGEGIDSDIMPHIFDRFRQADSSTrrshGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSA------ 385
Cdd:PRK15347  548 TVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFST-PGVGSCFSLVLPLNEyappep 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 386 ----VVA----------------EGHaQRPDTSAPRAA-------------------APRSEIDLS--GVRVLVVDDEPD 424
Cdd:PRK15347  623 lkgeLSAplalhrqlsawgitcqPGH-QNPALLDPELAylpgrlydllqqiiqgapnEPVINLPLQpwQLQILLVDDVET 701

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 425 GREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEGGRVPAMALTAFAREEDR 504
Cdd:PRK15347  702 NRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVALTANAAPEEI 781

                         410       420
                  ....*....|....*....|....*
gi 1232315758 505 LRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:PRK15347  782 HRCKKAGMNHYLTKPVTLAQLARAL 806

HK_WalK

NF033092

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...

163-383

1.89e-44

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.

Pssm-ID: 467964 [Multi-domain] Cd Length: 594 Bit Score: 166.08 E-value: 1.89e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 163 EFLATLSHELRTPLTAMLGWTQLLRSGALtADEEV--RGLEII----ERNVlaqaKLIDDLLDVSRIVTGKLRLNVRPLS 236
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALADGAW-KDPELapRFLGVTqnetERMI----RLVNDLLQLSRMDSKDYKLNKEWVN 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 237 LASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADE 316
Cdd:NF033092  449 FNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLLETHNRIIISISDQ 528

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232315758 317 GEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPL 383
Cdd:NF033092  529 GLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESE-EGKGTTIYFTLPY 594

REC_2_DhkD-like

cd17580

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...

416-525

3.56e-44

Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 152.23 E-value: 3.56e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeGGRVPAMAL 495
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW--LANTPAIAL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDEL 108

HATPase_c

smart00387

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

272-384

2.27e-39

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

Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 139.32 E-value: 2.27e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  272 GDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADsSTRRSHGGLGLGLA 351
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLGLS 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1232315758  352 IVRHVVELHGGSVRAESlGAGHGATFVVELPLS 384
Cdd:smart00387  80 IVKKLVELHGGEISVES-EPGGGTTFTITLPLE 111

CheY

COG0784

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...

410-538

1.41e-35

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];

Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 129.59 E-value: 1.41e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 410 DLSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapAEGGR 489
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAL--PRLPD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1232315758 490 VPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDAS 538
Cdd:COG0784    80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128

HATPase

cd00075

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...

277-381

3.42e-35

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.

Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 127.72 E-value: 3.42e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHV 356
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKS--REGGGTGLGLAIVRRI 78

                          90       100
                  ....*....|....*....|....*
gi 1232315758 357 VELHGGSVRAESlGAGHGATFVVEL 381
Cdd:cd00075    79 VEAHGGRITVES-EPGGGTTFTVTL 102

BaeS_SmeS

NF012163

sensor histidine kinase efflux regulator BaeS;

125-382

2.38e-34

sensor histidine kinase efflux regulator BaeS;

Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 135.34 E-value: 2.38e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 125 GDF------TSEDE--AVLLQLAQMASIAIENtlnseareaNRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEE 196
Cdd:NF012163  205 GDYttrvtpTSNDElgKLAQDFNQLASTLEKN---------EQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPE 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 197 vrGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDErAGHVTGDPDR 276
Cdd:NF012163  276 --SLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDR 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHV 356
Cdd:NF012163  353 LMQLFNNLLENSLRYTDSGGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNI 432

                         250       260
                  ....*....|....*....|....*.
gi 1232315758 357 VELHGGSVRAESLGAGhGATFVVELP 382
Cdd:NF012163  433 VQAHGGTLHAAHSPLG-GLRIVVTLP 457

HATPase_c

pfam02518

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...

272-383

3.83e-33

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: 122.09 E-value: 3.83e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 272 GDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLtRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSstrRSHGGLGLGLA 351
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLS 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 352 IVRHVVELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:pfam02518  77 IVRKLVELLGGTITVES-EPGGGTTVTLTLPL 107

MtrAB_MtrB

NF040691

MtrAB system histidine kinase MtrB;

130-385

2.50e-26

MtrAB system histidine kinase MtrB;

Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 112.43 E-value: 2.50e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 130 EDEAVLLQLA--QMASiAIENTLNsEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV-RGLEIIERN 206
Cdd:NF040691  240 EDDLARLARSfnQMAD-SLQRQIR-QLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDDFDPATaRSAELLHTE 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 207 VLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLV 286
Cdd:NF040691  318 LDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVV 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 287 NAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRA 366
Cdd:NF040691  398 NAIEHGE-GKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEA 476

                         250
                  ....*....|....*....
gi 1232315758 367 ESLgAGHGATFVVELPLSA 385
Cdd:NF040691  477 WGR-PGQGSQFRLTLPRVA 494

AdeS_HK

NF012226

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...

166-383

1.29e-24

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.

Pssm-ID: 411090 [Multi-domain] Cd Length: 353 Bit Score: 105.08 E-value: 1.29e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 166 ATLSHELRTPLTAMLGWTQLLRSGALTADeevrglEIIERNVLAQAK----LIDDLLDVSRIVTGKLRLNVRPLSLASVI 241
Cdd:NF012226  143 AAIAHELRTPITILQGRLQGILDGVFEPD------PALFKSLLNQVEglshLVEDLRTLSLVENQQLRLNYESVDLKDSI 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 242 EAALDVVRPAADAKavRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGID 321
Cdd:NF012226  217 EKVLKMFEDRLEQA--QLTIVLNLTATPVFCDRRRIEQVLIALIDNAIRYAN-AGKLKISSSVIQDDWILQIEDEGPGIA 293

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 322 SDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlgAGHGATFVVELPL 383
Cdd:NF012226  294 EEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSN--SQGNSVFTIKLPA 353

Response_reg

pfam00072

Response regulator receiver domain; This domain receives the signal from the sensor partner in ...

416-525

2.85e-23

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.

Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 94.53 E-value: 2.85e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMAL 495
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT----TPVIIL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPFDPDEL 106

PRK11361

acetoacetate metabolism transcriptional regulator AtoC;

415-525

4.25e-16

acetoacetate metabolism transcriptional regulator AtoC;

Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 80.66 E-value: 4.25e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMA 494
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET----RTPVIL 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112

REC

smart00448

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...

415-468

1.93e-11

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.

Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 59.12 E-value: 1.93e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1232315758  415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMP 468
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

GAF

pfam01590

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...

2-146

1.13e-04

Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 42.08 E-value: 1.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758   2 SMEKMLQVITDTAREIIGAHRATAvttWDQNWARCKTTLSLSPEFGPRRPLLSPSSGCELhtlwLALGRAgrLSSAELLA 81
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCAL---YLPDADGLEYLPPGARWLKAAGLEIPPGTGVTV----LRTGRP--LVVPDAAG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758  82 HPAWHTLGPSLCDFGqPPDWLAAPLTgRDGRDMGLLhVCGKCQGDFTSEDEAVLLQLAQMASIAI 146
Cdd:pfam01590  72 DPRFLDPLLLLRNFG-IRSLLAVPII-DDGELLGVL-VLHHPRPPFTEEELELLEVLADQVAIAL 133

GAF

smart00065

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...

7-150

2.77e-03

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.

Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 38.52 E-value: 2.77e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758    7 LQVITDTAREIIGAHRATAVTTWDQNWARCKTTLSlspeFGPRRPLLSPSSGCELHTLWLALGRAGRLSSAELLAHPAWH 86
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLVDENDRGELVLVAA----DGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758   87 tlGPSLCDFGQPPDWLAAPLTgRDGRDMGLLHVCGKCQGD-FTSEDEAVLLQLAQMASIAIENTL 150
Cdd:smart00065  82 --EDLLGRYQGVRSFLAVPLV-ADGELVGVLALHNKKSPRpFTEEDEELLQALANQLAIALANAQ 143

Name

Accession

Description

Interval

E-value

KdpD

COG2205

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

151-385

4.40e-85

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

Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 264.08 E-value: 4.40e-85

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 151 NSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSG-ALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLR 229
Cdd:COG2205     6 LEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLESGKLS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 230 LNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRS 309
Cdd:COG2205    86 LELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARREGDGV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 310 QIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSA 385
Cdd:COG2205   166 RISVSDNGPGIPEEELERIFERFYRGDNS--RGEGGTGLGLAIVKRIVEAHGGTIWVES-EPGGGTTFTVTLPLAE 238

WalK

COG5002

Sensor histidine kinase WalK [Signal transduction mechanisms];

152-384

8.22e-84

Sensor histidine kinase WalK [Signal transduction mechanisms];

Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 266.03 E-value: 8.22e-84

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 152 SEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV-RGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRL 230
Cdd:COG5002   156 TELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERrEYLEIILEEAERLSRLVNDLLDLSRLESGELKL 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 231 NVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQ 310
Cdd:COG5002   236 EKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVR 315

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232315758 311 IEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLS 384
Cdd:COG5002   316 ISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVES-EPGKGTTFTITLPLA 388

BaeS

COG0642

Signal transduction histidine kinase [Signal transduction mechanisms];

133-384

7.32e-80

Signal transduction histidine kinase [Signal transduction mechanisms];

Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 253.68 E-value: 7.32e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 133 AVLLQLAQMASIAIENTLNSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGAltADEEVRGLEIIERNVLAQAK 212
Cdd:COG0642    82 LLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEEL--DEEQREYLETILRSADRLLR 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 213 LIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFS 292
Cdd:COG0642   160 LINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYT 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 293 PVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHVVELHGGSVRAESlGAG 372
Cdd:COG0642   240 PEGGTVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVES-EPG 316

                         250
                  ....*....|..
gi 1232315758 373 HGATFVVELPLS 384
Cdd:COG0642   317 KGTTFTVTLPLA 328

TMAO_torS

TIGR02956

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...

153-531

9.99e-60

Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 213.49 E-value: 9.99e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 153 EAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTAdEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNV 232
Cdd:TIGR02956 456 EAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTS-QQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISP 534

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 233 RPLSLASVIEAALDVVRPAADAKAVRfepLLDERAGHVT----GDPDRLQQVVWNLLVNAVKFSPVGG-KIRVSLTRQGS 307
Cdd:TIGR02956 535 RPFDLNALLDDVHHLMVSRAQLKGIQ---LRLNIPEQLPnwwqGDGPRIRQVLINLVGNAIKFTDRGSvVLRVSLNDDSS 611

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 308 RSqIEVADEGEGIDSDIMPHIFDRFRQADSstRRSHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSavv 387
Cdd:TIGR02956 612 LL-FEVEDTGCGIAEEEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESE-LGVGSCFWFTLPLT--- 684

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 388 aegHAQRPDTSAPRAAaprseIDLSGVRVLVVDDEP-DGREAIAKVLSVYHaQVATASSAREALALFAQARPDVLISDIG 466
Cdd:TIGR02956 685 ---RGKPAEDSATLTV-----IDLPPQRVLLVEDNEvNQMVAQGFLTRLGH-KVTLAESGQSALECFHQHAFDLALLDIN 755

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758 467 MPEEDGYDLIRRVRDLAPAEgGRVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:TIGR02956 756 LPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819

PRK15347

two component system sensor kinase;

153-529

2.70e-51

two component system sensor kinase;

Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 189.08 E-value: 2.70e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 153 EAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTAdEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNV 232
Cdd:PRK15347  390 RAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTA-EQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSL 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 233 RPLSLASVIEAALDVVRPAADAKAVRFEPLL-DERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGkIRVSLTRQGSRSQI 311
Cdd:PRK15347  469 EETALLPLLDQAMLTIQGPAQSKSLTLRTFVgAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG-IRLRVKRHEQQLCF 547

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 312 EVADEGEGIDSDIMPHIFDRFRQADSSTrrshGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSA------ 385
Cdd:PRK15347  548 TVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFST-PGVGSCFSLVLPLNEyappep 622

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 386 ----VVA----------------EGHaQRPDTSAPRAA-------------------APRSEIDLS--GVRVLVVDDEPD 424
Cdd:PRK15347  623 lkgeLSAplalhrqlsawgitcqPGH-QNPALLDPELAylpgrlydllqqiiqgapnEPVINLPLQpwQLQILLVDDVET 701

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 425 GREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEGGRVPAMALTAFAREEDR 504
Cdd:PRK15347  702 NRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDPDCMIVALTANAAPEEI 781

                         410       420
                  ....*....|....*....|....*
gi 1232315758 505 LRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:PRK15347  782 HRCKKAGMNHYLTKPVTLAQLARAL 806

NtrY

COG5000

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...

163-385

4.35e-46

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: 167.06 E-value: 4.35e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 163 EFLATLSHELRTPLTAMLGWTQLLR---SGALTADEEV--RGLEIIERNVLAQAKLIDDLLDVSRIvtgkLRLNVRPLSL 237
Cdd:COG5000   203 ELARRIAHEIKNPLTPIQLSAERLRrklADKLEEDREDleRALDTIIRQVDRLKRIVDEFLDFARL----PEPQLEPVDL 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 238 ASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEG 317
Cdd:COG5000   279 NELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEVSDNG 358

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232315758 318 EGIDSDIMPHIFDRFrqadSSTRRShgGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSA 385
Cdd:COG5000   359 PGIPEEVLERIFEPF----FTTKPK--GTGLGLAIVKKIVEEHGGTIELESR-PGGGTTFTIRLPLAE 419

phoR_proteo

TIGR02966

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...

152-377

2.87e-45

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]

Pssm-ID: 274368 [Multi-domain] Cd Length: 333 Bit Score: 162.76 E-value: 2.87e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 152 SEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV-RGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRL 230
Cdd:TIGR02966 105 TRLRRLEQMRRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWnRALEIMLEQSQRMQSLVEDLLTLSRLESAASPL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 231 NVRPLSLASVIEAALDVVRPAADAKAVRFEpLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQ 310
Cdd:TIGR02966 185 EDEPVDMPALLDHLRDEAEALSQGKNHQIT-FEIDGGVDVLGDEDELRSAFSNLVSNAIKYTPEGGTITVRWRRDGGGAE 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232315758 311 IEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATF 377
Cdd:TIGR02966 264 FSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIES-ELGKGSTF 329

COG4251

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...

150-385

1.05e-44

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

Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 165.34 E-value: 1.05e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 150 LNSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLL-RSGALTADEEVRG-LEIIERNVLAQAKLIDDLLDVSRIvtGK 227
Cdd:COG4251   271 RTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLeEDYGDKLDEEGREyLERIRDAAERMQALIDDLLAYSRV--GR 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 228 LRLNVRPLSLASVIEAALDVVRPAADAKAVRFE--PLLderagHVTGDPDRLQQVVWNLLVNAVKFSPVG--GKIRVSLT 303
Cdd:COG4251   349 QELEFEPVDLNELLEEVLEDLEPRIEERGAEIEvgPLP-----TVRGDPTLLRQVFQNLISNAIKYSRPGepPRIEIGAE 423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 304 RQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSstRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:COG4251   424 REGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVES-EPGEGATFYFTLPK 500


                  ..
gi 1232315758 384 SA 385
Cdd:COG4251   501 AP 502

HK_WalK

NF033092

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...

163-383

1.89e-44

Pssm-ID: 467964 [Multi-domain] Cd Length: 594 Bit Score: 166.08 E-value: 1.89e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 163 EFLATLSHELRTPLTAMLGWTQLLRSGALtADEEV--RGLEII----ERNVlaqaKLIDDLLDVSRIVTGKLRLNVRPLS 236
Cdd:NF033092  374 EFVANVSHELRTPLTTMRSYLEALADGAW-KDPELapRFLGVTqnetERMI----RLVNDLLQLSRMDSKDYKLNKEWVN 448

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 237 LASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADE 316
Cdd:NF033092  449 FNEFFNYIIDRFEMILKNKNITFKREFPKRDLWVEIDTDKITQVLDNIISNAIKYSPEGGTITFRLLETHNRIIISISDQ 528

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232315758 317 GEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPL 383
Cdd:NF033092  529 GLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESE-EGKGTTIYFTLPY 594

COG4191

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...

132-384

2.09e-44

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

Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 161.12 E-value: 2.09e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 132 EAVLLQLAQMASIAientlnseareanrikdEFLATLSHELRTPLTAMLGWTQLLR---SGALTADEEVRGLEIIERNVL 208
Cdd:COG4191   130 QEQLVQSEKLAALG-----------------ELAAGIAHEINNPLAAILGNAELLRrrlEDEPDPEELREALERILEGAE 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 209 AQAKLIDDLLDVSRivtgKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNA 288
Cdd:COG4191   193 RAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINA 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 289 VKFSP--VGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRSHGGLGLGLAIVRHVVELHGGSVRA 366
Cdd:COG4191   269 IDAMEegEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPF----FTTKPVGKGTGLGLSISYGIVEKHGGRIEV 344

                         250
                  ....*....|....*...
gi 1232315758 367 ESlGAGHGATFVVELPLS 384
Cdd:COG4191   345 ES-EPGGGTTFTITLPLA 361

REC_2_DhkD-like

cd17580

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...

416-525

3.56e-44

Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 152.23 E-value: 3.56e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeGGRVPAMAL 495
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW--LANTPAIAL 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17580    79 TGYGQPEDRERALEAGFDAHLVKPVDPDEL 108

PRK11107

hybrid sensory histidine kinase BarA; Provisional

153-485

4.43e-44

hybrid sensory histidine kinase BarA; Provisional

Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 167.72 E-value: 4.43e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 153 EAREANRIKDEFLATLSHELRTPLTAMLGWT-QLLRSgALTADEeVRGLEIIER---NVLAqakLIDDLLDVSRIVTGKL 228
Cdd:PRK11107  285 RAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKT-PLTPTQ-RDYLQTIERsanNLLA---IINDILDFSKLEAGKL 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 229 RLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERA-GHVTGDPDRLQQVVWNLLVNAVKFSPVGG-KIRVSLTRQG 306
Cdd:PRK11107  360 VLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVpDNVIGDPLRLQQIITNLVGNAIKFTESGNiDILVELRALS 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 307 SRS---QIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:PRK11107  440 NTKvqlEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHS-QPNRGSTFWFHLPL 518

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 384 savvaeghaqrpDTSaPRAAAPRSEID-LSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSareaLALFAQARPDVLI 462
Cdd:PRK11107  519 ------------DLN-PNPIIDGLPTDcLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSPT----LSQLPEAHYDILL 581

                         330       340
                  ....*....|....*....|...
gi 1232315758 463 sdIGMPEEDGYDLIRRVRDLAPA 485
Cdd:PRK11107  582 --LGLPVTFREPLTMLHERLAKA 602

NtrB

COG3852

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

132-384

7.19e-43

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

Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 156.93 E-value: 7.19e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 132 EAVLLQLAQMASIAientlnseareanrikdEFLATLSHELRTPLTAMLGWTQLLRSgALTADEEVRGLEIIERNVLAQA 211
Cdd:COG3852   123 ERELRRAEKLAAVG-----------------ELAAGLAHEIRNPLTGIRGAAQLLER-ELPDDELREYTQLIIEEADRLN 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 212 KLIDDLLDVSRivtgKLRLNVRPLSLASVIEAALDVVRPAAdAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKF 291
Cdd:COG3852   185 NLVDRLLSFSR----PRPPEREPVNLHEVLERVLELLRAEA-PKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEA 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 292 SPVGGKIRVSL----------TRQGSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRshGGLGLGLAIVRHVVELHG 361
Cdd:COG3852   260 MPEGGTITIRTrverqvtlggLRPRLYVRIEVIDNGPGIPEEILDRIFEPF----FTTKE--KGTGLGLAIVQKIVEQHG 333

                         250       260
                  ....*....|....*....|...
gi 1232315758 362 GSVRAESlGAGHGATFVVELPLS 384
Cdd:COG3852   334 GTIEVES-EPGKGTTFRIYLPLE 355

HATPase_c

smart00387

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

272-384

2.27e-39

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

Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 139.32 E-value: 2.27e-39

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  272 GDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADsSTRRSHGGLGLGLA 351
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTD-KRSRKIGGTGLGLS 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1232315758  352 IVRHVVELHGGSVRAESlGAGHGATFVVELPLS 384
Cdd:smart00387  80 IVKKLVELHGGEISVES-EPGGGTTFTITLPLE 111

PRK11466

hybrid sensory histidine kinase TorS; Provisional

132-530

7.73e-38

hybrid sensory histidine kinase TorS; Provisional

Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 149.29 E-value: 7.73e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 132 EAVLLQLAQMASIAIEN-TLNSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTAD--EEVRGLEIIERNVL 208
Cdd:PRK11466  414 AQVKARTAELQELVIEHrQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAqrDDLRAITDSGESLL 493

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 209 AqakLIDDLLDVSRIVTG--KLRLNVRPLSLASVIEAALDVVRPAADAKAVRF-EPLLDERAGHVTGDPDRLQQVVWNLL 285
Cdd:PRK11466  494 T---ILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLaTDIADDLPTALMGDPRRIRQVITNLL 570

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 286 VNAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQAdsSTRRshGGLGLGLAIVRHVVELHGGSVR 365
Cdd:PRK11466  571 SNALRFTD-EGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQV--SGKR--GGTGLGLTISSRLAQAMGGELS 645

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 366 AESLgAGHGATFVVELPLsavvaeghaQRPdtSAPRAAAPRSEIDLSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASS 445
Cdd:PRK11466  646 ATST-PEVGSCFCLRLPL---------RVA--TAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGN 713

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 446 AREALALFAQARP-DVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAE 524
Cdd:PRK11466  714 AAQALETLQNSEPfAAALVDFDLPDYDGITLARQLAQQYPS----LVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREV 789


                  ....*.
gi 1232315758 525 LAAGVA 530
Cdd:PRK11466  790 LGQLLA 795

PRK09959

acid-sensing system histidine kinase EvgS;

152-532

2.60e-37

acid-sensing system histidine kinase EvgS;

Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 147.96 E-value: 2.60e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  152 SEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLN 231
Cdd:PRK09959   703 NKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLIGEILDVDKIESGNYQLQ 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  232 VRPLSLASVIEAALDVVRPAADAKAVRFEpLLDERAGH--VTGDPDRLQQVVWNLLVNAVKFSPVGG-KIRVSLTRQGSR 308
Cdd:PRK09959   783 PQWVDIPTLVQNTCHSFGAIAASKSIALS-CSSTFPDHylVKIDPQAFKQVLSNLLSNALKFTTEGAvKITTSLGHIDDN 861

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  309 S---QIEVADEGEGIDSDIMPHIFDRFRQadSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSA 385
Cdd:PRK09959   862 HaviKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLES-HPGIGTTFTITIPVEI 938

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  386 V----VAEGHAQRPDTSAPRaaaprseidlsgVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVL 461
Cdd:PRK09959   939 SqqvaTVEAKAEQPITLPEK------------LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLL 1006

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232315758  462 ISDIGMPEEDGYDLIRRVRDlapaEGGRVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:PRK09959  1007 ITDVNMPNMDGFELTRKLRE----QNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQL 1073

PRK10841

two-component system sensor histidine kinase RcsC;

152-520

1.04e-36

two-component system sensor histidine kinase RcsC;

Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 145.89 E-value: 1.04e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 152 SEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADeevrgleiIERNVLAQA-------KLIDDLLDVSRIV 224
Cdd:PRK10841  438 QAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKG--------VDRLVTAMNnssslllKIISDILDFSKIE 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 225 TGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRF----EPLLDERaghVTGDPDRLQQVVWNLLVNAVKFSPVGGkIRV 300
Cdd:PRK10841  510 SEQLKIEPREFSPREVINHITANYLPLVVKKRLGLycfiEPDVPVA---LNGDPMRLQQVISNLLSNAIKFTDTGC-IVL 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 301 SLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVE 380
Cdd:PRK10841  586 HVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDS-EPGMGSQFTIR 664

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 381 LPL---------------------------------------SAVVAEGHAQRPDTS----------------------- 398
Cdd:PRK10841  665 IPLygaqypqkkgveglqgkrcwlavrnasleqfletllqrsGIQVQRYEGQEPTPEdvlitddpvqkkwqgravitfcr 744

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 399 ----APRAAAP---------------------RSEIDLSG-----------------VRVLVVDDEPDGREAIAKVLSVY 436
Cdd:PRK10841  745 rhigIPLEIAPgewvhstatphelpallariyRIELESDDsanalpstdkavsdnddMMILVVDDHPINRRLLADQLGSL 824

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 437 HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapaeGGRVPAMALTAFAREEDRLRAIEAGFQVHA 516
Cdd:PRK10841  825 GYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL----GLTLPVIGVTANALAEEKQRCLEAGMDSCL 900


                  ....
gi 1232315758 517 IKPV 520
Cdd:PRK10841  901 SKPV 904

CheY

COG0784

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...

410-538

1.41e-35

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];

Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 129.59 E-value: 1.41e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 410 DLSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapAEGGR 489
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRAL--PRLPD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1232315758 490 VPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDAS 538
Cdd:COG0784    80 IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128

PRK11091

aerobic respiration control sensor protein ArcB; Provisional

157-540

2.50e-35

aerobic respiration control sensor protein ArcB; Provisional

Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 141.23 E-value: 2.50e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 157 ANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTaDEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLS 236
Cdd:PRK11091  279 ASRDKTTFISTISHELRTPLNGIVGLSRILLDTELT-AEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPID 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 237 LASVIEAALDVVRPAADAKAVRF--EPLLDERAgHVTGDPDRLQQVVWNLLVNAVKFSPVGG-KIRVSLTrQGSRSQIEV 313
Cdd:PRK11091  358 FTDFLADLENLSGLQAEQKGLRFdlEPLLPLPH-KVITDGTRLRQILWNLISNAVKFTQQGGvTVRVRYE-EGDMLTFEV 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 314 ADEGEGIDSDIMPHIFDRFRQA-DSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLsAVVAEGHA 392
Cdd:PRK11091  436 EDSGIGIPEDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTS-EEGKGSCFTLTIHA-PAVAEEVE 513

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 393 QRPDTsapraaaprSEIDLSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDG 472
Cdd:PRK11091  514 DAFDE---------DDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTG 584

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232315758 473 YDLIRRVRDLAPAEgGRVPAMALTAFAReEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPS 540
Cdd:PRK11091  585 LDIARELRERYPRE-DLPPLVALTANVL-KDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEE 650

cztS_silS_copS

TIGR01386

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...

164-382

2.58e-35

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.

Pssm-ID: 273593 [Multi-domain] Cd Length: 457 Bit Score: 137.90 E-value: 2.58e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 164 FLATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLE--IIERNVLAqaKLIDDLLDVSRIVTGKLRLNVRPLSLASVI 241
Cdd:TIGR01386 244 FSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLEsnLEELERLS--RMVSDMLFLARADNGQLALERVRLDLAAEL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 242 EAALDVVRPAADAKAVRfepLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGID 321
Cdd:TIGR01386 322 AKVAEYFEPLAEERGVR---IRVEGEGLVRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRVSVSNPGPGIP 398

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232315758 322 SDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlgAGHGATFVVELP 382
Cdd:TIGR01386 399 PEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAES--PDGKTRFILRFP 457

HATPase

cd00075

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...

277-381

3.42e-35

Pssm-ID: 340391 [Multi-domain] Cd Length: 102 Bit Score: 127.72 E-value: 3.42e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHV 356
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKS--REGGGTGLGLAIVRRI 78

                          90       100
                  ....*....|....*....|....*
gi 1232315758 357 VELHGGSVRAESlGAGHGATFVVEL 381
Cdd:cd00075    79 VEAHGGRITVES-EPGGGTTFTVTL 102

PRK11100

sensory histidine kinase CreC; Provisional

167-385

3.93e-35

sensory histidine kinase CreC; Provisional

Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 137.67 E-value: 3.93e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 167 TLSHELRTPLTAMLGWTQLLRsGALTADEEVRGLEiierNVLAQAK----LIDDLLDVSRIVTGKLRLNVRPLSLASVIE 242
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAELLQ-EDPPPEDRARFTG----NILTQSArlqqLIDRLLELARLEQRQELEVLEPVALAALLE 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 243 AALDVVRPAADAKAVRFEPLLDERAghVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDS 322
Cdd:PRK11100  337 ELVEAREAQAAAKGITLRLRPDDAR--VLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIPD 414

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 323 DIMPHIFDRFrqadSSTRRSHGGL---GLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSA 385
Cdd:PRK11100  415 YALPRIFERF----YSLPRPANGRkstGLGLAFVREVARLHGGEVTLRNR-PEGGVLATLTLPRHF 475

BaeS_SmeS

NF012163

sensor histidine kinase efflux regulator BaeS;

125-382

2.38e-34

sensor histidine kinase efflux regulator BaeS;

Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 135.34 E-value: 2.38e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 125 GDF------TSEDE--AVLLQLAQMASIAIENtlnseareaNRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEE 196
Cdd:NF012163  205 GDYttrvtpTSNDElgKLAQDFNQLASTLEKN---------EQMRRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPE 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 197 vrGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDErAGHVTGDPDR 276
Cdd:NF012163  276 --SLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPD-SSLVFGDRDR 352

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHV 356
Cdd:NF012163  353 LMQLFNNLLENSLRYTDSGGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNI 432

                         250       260
                  ....*....|....*....|....*.
gi 1232315758 357 VELHGGSVRAESLGAGhGATFVVELP 382
Cdd:NF012163  433 VQAHGGTLHAAHSPLG-GLRIVVTLP 457

HATPase_EvgS-ArcB-TorS-like

cd16922

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...

277-383

1.26e-33

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: 123.37 E-value: 1.26e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGG-KIRVSLTRQGSRS---QIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAI 352
Cdd:cd16922     1 LRQILLNLLGNAIKFTEEGEvTLRVSLEEEEEDGvqlRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 353 VRHVVELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:cd16922    81 SKKLVELMGGDISVES-EPGQGSTFTFTLPL 110

PRK09303

histidine kinase;

130-382

3.45e-33

histidine kinase;

Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 130.46 E-value: 3.45e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 130 EDEavLLQLAQmasiaiEN-TLnseaREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV----------- 197
Cdd:PRK09303  131 SDE--LFVLRQ------ENeTL----LEQLKFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELkpalieqlqdq 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 198 --RGLEIIERnvlaqakLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFE-------PLlderag 268
Cdd:PRK09303  199 arRQLEEIER-------LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQtdipsdlPS------ 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 269 hVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVS-LTRQGSRSQIEVADEGEGIDSDIMPHIF-DRFR-QADSSTRrshgG 345
Cdd:PRK09303  266 -VYADQERIRQVLLNLLDNAIKYTPEGGTITLSmLHRTTQKVQVSICDTGPGIPEEEQERIFeDRVRlPRDEGTE----G 340

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1232315758 346 LGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELP 382
Cdd:PRK09303  341 YGIGLSVCRRIVRVHYGQIWVDS-EPGQGSCFHFTLP 376

HATPase_c

pfam02518

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...

272-383

3.83e-33

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: 122.09 E-value: 3.83e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 272 GDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLtRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSstrRSHGGLGLGLA 351
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITVTL-SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLS 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 352 IVRHVVELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:pfam02518  77 IVRKLVELLGGTITVES-EPGGGTTVTLTLPL 107

PRK10549

two-component system sensor histidine kinase BaeS;

125-383

4.83e-32

two-component system sensor histidine kinase BaeS;

Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 128.98 E-value: 4.83e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 125 GDFT------SEDEavLLQLA----QMASiaienTL--NSEAREAnrikdeFLATLSHELRTPLTAMLGWTQLLRSGALT 192
Cdd:PRK10549  205 GDFTtrvtptSRDE--LGRLAqdfnQLAS-----TLekNEQMRRD------FMADISHELRTPLAVLRGELEAIQDGVRK 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 193 ADEEvrGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAgHVTG 272
Cdd:PRK10549  272 FTPE--SVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSA-TVFG 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAI 352
Cdd:PRK10549  349 DPDRLMQLFNNLLENSLRYTDSGGSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1232315758 353 VRHVVELHGGSVRAESLGAGhGATFVVELPL 383
Cdd:PRK10549  429 CLNIVEAHNGRIIAAHSPFG-GVSITVELPL 458

KinE

COG5809

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...

163-384

1.20e-31

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: 128.17 E-value: 1.20e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 163 EFLATLSHELRTPLTAMLGWTQLLRSGALtaDEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKlrlnVRPLSLASVIE 242
Cdd:COG5809   272 ELAAGIAHEIRNPLTSLKGFIQLLKDTID--EEQKTYLDIMLSELDRIESIISEFLVLAKPQAIK----YEPKDLNTLIE 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 243 AALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQ-GSRSQIEVADEGEGID 321
Cdd:COG5809   346 EVIPLLQPQALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAEdDDKVVISVTDEGCGIP 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315758 322 SDIMPHIFDRFrqadSSTRrsHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLS 384
Cdd:COG5809   426 EERLKKLGEPF----YTTK--EKGTGLGLMVSYKIIEEHGGKITVESE-VGKGTTFSITLPIK 481

PRK10490

sensor protein KdpD; Provisional

136-386

4.28e-31

sensor protein KdpD; Provisional

Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 128.62 E-value: 4.28e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 136 LQLAQMASIAienTLNSEaREanRIKDEFLATLSHELRTPLTAMLGWTQLLR-SGALTADEEVRGLEIIERNVLAQAKLI 214
Cdd:PRK10490  645 LTLTASEEQA---RLASE-RE--QLRNALLAALSHDLRTPLTVLFGQAEILTlDLASEGSPHARQASEIRQQVLNTTRLV 718

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 215 DDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEplLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPV 294
Cdd:PRK10490  719 NNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLS--LPEPLTLIHVDGPLFERVLINLLENAVKYAGA 796

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 295 GGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTrrSHGGLGLGLAIVRHVVELHGGSVRAESLGAGhG 374
Cdd:PRK10490  797 QAEIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNKES--AIPGVGLGLAICRAIVEVHGGTIWAENRPEG-G 873

                         250
                  ....*....|..
gi 1232315758 375 ATFVVELPLSAV 386
Cdd:PRK10490  874 ACFRVTLPLETP 885

PRK11360

two-component system sensor histidine kinase AtoS;

163-383

2.85e-30

two-component system sensor histidine kinase AtoS;

Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 125.08 E-value: 2.85e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 163 EFLATLSHELRTPLTAMLGWTQLLRSGAlTADEEVRGLEIIERNVLAQAKLIDDLLDVSRivtgKLRLNVRPLSLASVIE 242
Cdd:PRK11360  392 ELVAGVAHEIRNPLTAIRGYVQIWRQQT-SDPPSQEYLSVVLREVDRLNKVIDQLLEFSR----PRESQWQPVSLNALVE 466

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 243 AALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQ-IEVADEGEGID 321
Cdd:PRK11360  467 EVLQLFQTAGVQARVDFETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYSDGQVaVSIEDNGCGID 546

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 322 SDIMPHIFDRFrqadSSTRRShgGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPL 383
Cdd:PRK11360  547 PELLKKIFDPF----FTTKAK--GTGLGLALSQRIINAHGGDIEVESE-PGVGTTFTLYLPI 601

HATPase_TutC-TodS-like

cd16925

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...

273-382

4.99e-30

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.

Pssm-ID: 340402 [Multi-domain] Cd Length: 110 Bit Score: 113.74 E-value: 4.99e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTR-QGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLA 351
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKfRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLS 80

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 352 IVRHVVELHGGSVRAeSLGAGHGATFVVELP 382
Cdd:cd16925    81 IVKEFVELHGGTVTV-SDAPGGGALFQVELP 110

PRK10604

sensor protein RstB; Provisional

168-383

2.14e-29

sensor protein RstB; Provisional

Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 120.48 E-value: 2.14e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 168 LSHELRTPLtAMLGWtQLLRSGALTADEEvrglEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDV 247
Cdd:PRK10604  219 IAHELRTPL-VRLRY-RLEMSDNLSAAES----QALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLAD 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 248 VRPAADAKAVRFEPLLDERAGhvTGDPDRLQQVVWNLLVNAVKFSpvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPH 327
Cdd:PRK10604  293 IQAVTPEKTVRLDTPHQGDYG--ALDMRLMERVLDNLLNNALRYA--HSRVRVSLLLDGNQACLIVEDDGPGIPPEERER 368

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 328 IFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESLGAGhGATFVVELPL 383
Cdd:PRK10604  369 VFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELG-GARFSFSWPV 423

OmpR

COG0745

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...

415-545

4.17e-29

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];

Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 114.28 E-value: 4.17e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMA 494
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLR----ARPSDIPIIM 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPSGPNGD 545
Cdd:COG0745    79 LTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVLRVGD 129

RpfG

COG3437

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...

415-532

1.17e-28

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];

Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 113.72 E-value: 1.17e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEggRVPAMA 494
Cdd:COG3437     8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTR--DIPVIF 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:COG3437    86 LTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123

PleD

COG3706

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...

415-533

3.84e-27

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];

Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 108.07 E-value: 3.84e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapAEGGRVPAMA 494
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRAD--PRTADIPIIF 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLA 533
Cdd:COG3706    81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVA 119

MtrAB_MtrB

NF040691

MtrAB system histidine kinase MtrB;

130-385

2.50e-26

MtrAB system histidine kinase MtrB;

Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 112.43 E-value: 2.50e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 130 EDEAVLLQLA--QMASiAIENTLNsEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV-RGLEIIERN 206
Cdd:NF040691  240 EDDLARLARSfnQMAD-SLQRQIR-QLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDDFDPATaRSAELLHTE 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 207 VLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLV 286
Cdd:NF040691  318 LDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVV 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 287 NAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRA 366
Cdd:NF040691  398 NAIEHGE-GKPVVVTVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEA 476

                         250
                  ....*....|....*....
gi 1232315758 367 ESLgAGHGATFVVELPLSA 385
Cdd:NF040691  477 WGR-PGQGSQFRLTLPRVA 494

HATPase_BaeS-like

cd16946

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

273-382

5.33e-26

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.

Pssm-ID: 340422 [Multi-domain] Cd Length: 109 Bit Score: 102.16 E-value: 5.33e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAI 352
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 353 VRHVVELHGGSVRAESLGAGhGATFVVELP 382
Cdd:cd16946    81 CHNIALAHGGTISAEHSPLG-GLRLVLTLP 109

PRK10364

two-component system sensor histidine kinase ZraS;

166-385

6.05e-26

two-component system sensor histidine kinase ZraS;

Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 110.65 E-value: 6.05e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 166 ATLSHELRTPLTAMLGWTQLL--RSGALTADEEVRGLEIIERNVLAqaKLIDDLLDVSRivtgKLRLNVRPLSLASVIEA 243
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFaeRAPAGGEAHQLAQVMAKEADRLN--RVVSELLELVK----PTHLALQAVDLNDLINH 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 244 ALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSD 323
Cdd:PRK10364  316 SLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAAD 395

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 324 IMPHIFDRFRQADSStrrshgGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSA 385
Cdd:PRK10364  396 QLEAIFTPYFTTKAE------GTGLGLAVVHNIVEQHGGTIQVASQ-EGKGATFTLWLPVNI 450

PRK09835

Cu(+)/Ag(+) sensor histidine kinase;

155-382

1.95e-25

Cu(+)/Ag(+) sensor histidine kinase;

Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 109.48 E-value: 1.95e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 155 REANrikdeFLATLSHELRTPLTAMLGWTQLLRSGALTADE--EV--RGLEIIERnvlaQAKLIDDLLDVSRIVTGKLRL 230
Cdd:PRK09835  261 RQSN-----FSADIAHEIRTPITNLITQTEIALSQSRSQKEleDVlySNLEELTR----MAKMVSDMLFLAQADNNQLIP 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 231 NVRPLSLASVIEAALDVVRPAADAKAVRFEplLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQ 310
Cdd:PRK09835  332 EKKMLDLADEVGKVFDFFEAWAEERGVELR--FVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEVDHQVQ 409

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 311 IEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlgAGHGATFVVELP 382
Cdd:PRK09835  410 LVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTS--DARGTRFVISLP 479

PRK13557

histidine kinase; Provisional

168-546

4.31e-25

histidine kinase; Provisional

Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 108.99 E-value: 4.31e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 168 LSHELRTPLTAMLGWTQLLRSGA----LTADEEVRGLEIIERNVLAQAKLIDDLLDVSRivtgKLRLNVRPLSLASVIEA 243
Cdd:PRK13557  170 IAHDFNNLLQVMSGYLDVIQAALshpdADRGRMARSVENIRAAAERAATLTQQLLAFAR----KQRLEGRVLNLNGLVSG 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 244 ALDVVRPAAdAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVS-----LTRQGSRSQ-------- 310
Cdd:PRK13557  246 MGELAERTL-GDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRtrnveIEDEDLAMYhglppgry 324

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 311 --IEVADEGEGIDSDIMPHIFDRFrqadSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPlsavVA 388
Cdd:PRK13557  325 vsIAVTDTGSGMPPEILARVMDPF----FTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYS-EVGEGTTVRLYFP----AS 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 389 EGHAQRPDTSAPRAAA-PRSEidlsgvRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQ-ARPDVLISDIG 466
Cdd:PRK13557  396 DQAENPEQEPKARAIDrGGTE------TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDShPEVDLLFTDLI 469

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 467 MP-EEDGYDLIRRVRDLAPaeggRVPAMALTAFAREE-DRLRAIEAGFQVHAiKPVQPAELAAGVAKLAgrdaspSGPNG 544
Cdd:PRK13557  470 MPgGMNGVMLAREARRRQP----KIKVLLTTGYAEASiERTDAGGSEFDILN-KPYRRAELARRVRMVL------DGPTG 538


                  ..
gi 1232315758 545 DG 546
Cdd:PRK13557  539 VG 540

REC

cd00156

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...

417-519

6.08e-25

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 98.84 E-value: 6.08e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 417 LVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMALT 496
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD----IPVIVLT 76

                          90       100
                  ....*....|....*....|...
gi 1232315758 497 AFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd00156    77 AKADEEDAVRALELGADDYLVKP 99

AtoC

COG2204

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...

415-557

1.21e-24

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];

Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 106.59 E-value: 1.21e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMA 494
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP----DLPVIL 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPSGPNGDGHGVSANPLIMA 557
Cdd:COG2204    80 LTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRENAEDSGLIGRSPAMQE 142

AdeS_HK

NF012226

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...

166-383

1.29e-24

Pssm-ID: 411090 [Multi-domain] Cd Length: 353 Bit Score: 105.08 E-value: 1.29e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 166 ATLSHELRTPLTAMLGWTQLLRSGALTADeevrglEIIERNVLAQAK----LIDDLLDVSRIVTGKLRLNVRPLSLASVI 241
Cdd:NF012226  143 AAIAHELRTPITILQGRLQGILDGVFEPD------PALFKSLLNQVEglshLVEDLRTLSLVENQQLRLNYESVDLKDSI 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 242 EAALDVVRPAADAKavRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGID 321
Cdd:NF012226  217 EKVLKMFEDRLEQA--QLTIVLNLTATPVFCDRRRIEQVLIALIDNAIRYAN-AGKLKISSSVIQDDWILQIEDEGPGIA 293

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 322 SDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESlgAGHGATFVVELPL 383
Cdd:NF012226  294 EEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSN--SQGNSVFTIKLPA 353

REC_hyHK_CKI1_RcsC-like

cd17546

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...

416-525

2.53e-24

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 97.54 E-value: 2.53e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLaPAEGGRVPAMAL 495
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIREL-EGGGRRTPIIAL 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17546    80 TANALEEDREKCLEAGMDDYLSKPVKLDQL 109

phoR

PRK11006

phosphate regulon sensor histidine kinase PhoR;

164-387

5.60e-24

phosphate regulon sensor histidine kinase PhoR;

Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 104.71 E-value: 5.60e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 164 FLATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLrlnvrpLSLASVIE- 242
Cdd:PRK11006  207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPT------IDLNEKVDv 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 243 -AALDVVRPAADA-----KAVRFEplLDERAgHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADE 316
Cdd:PRK11006  281 pMMLRVLEREAQTlsqgkHTITFE--VDNSL-KVFGNEDQLRSAISNLVYNAVNHTPEGTHITVRWQRVPQGAEFSVEDN 357

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232315758 317 GEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSAVV 387
Cdd:PRK11006  358 GPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESE-VGKGTRFSFVLPERLIA 427

KinB

COG5806

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...

138-384

6.38e-24

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

Pssm-ID: 444508 [Multi-domain] Cd Length: 412 Bit Score: 104.18 E-value: 6.38e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 138 LAQMASIAIENTLNSEAREANRIKDEFL------------ATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLEI--- 202
Cdd:COG5806   166 IIQLLAMLIAVYLIENLIENILLRKELQraeklevvselaASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIale 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 203 -IERnvlAQAkLIDDLLDVSRIVTGKLrlnvRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAgHVTGDPDRLQQVV 281
Cdd:COG5806   246 eLDR---AEA-IITDYLTFAKPQPEKL----EKIDVSEELEHVIDVLSPYANMNNVEIQTELEPGL-YIEGDRQKLQQCL 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 282 WNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDimpHIfDRFRQADSSTRRShgGLGLGLAIVRHVVELHG 361
Cdd:COG5806   317 INIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKDTGVGMTKE---QL-ERLGEPYFSTKEK--GTGLGTMVSYRIIEAMN 390

                         250       260
                  ....*....|....*....|...
gi 1232315758 362 GSVRAESLgAGHGATFVVELPLS 384
Cdd:COG5806   391 GTIRVESE-VGKGTTFTITLPLA 412

YesN

COG4753

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...

415-511

6.48e-24

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];

Pssm-ID: 443786 [Multi-domain] Cd Length: 103 Bit Score: 96.00 E-value: 6.48e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVY--HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPA 492
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDP----DTKI 76

                          90
                  ....*....|....*....
gi 1232315758 493 MALTAFAREEDRLRAIEAG 511
Cdd:COG4753    77 IILSGYSDFEYAQEAIKLG 95

Response_reg

pfam00072

Response regulator receiver domain; This domain receives the signal from the sensor partner in ...

416-525

2.85e-23

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.

Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 94.53 E-value: 2.85e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMAL 495
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT----TPVIIL 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:pfam00072  77 TAHGDEDDAVEALEAGADDFLSKPFDPDEL 106

PRK13837

two-component system VirA-like sensor kinase;

168-530

5.31e-23

two-component system VirA-like sensor kinase;

Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 103.60 E-value: 5.31e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 168 LSHELRTPLTAMLGWTQL----LRSGALTADEEvrgLEIIERNVLAQaKLIDDLLDVSRivtgKLRLNVRPLSLASVIEA 243
Cdd:PRK13837  457 IAHNFNNILGAILGYAEMalnkLARHSRAARYI---DEIISAGARAR-LIIDQILAFGR----KGERNTKPFDLSELVTE 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 244 ALDVVRpAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQ---------------GSR 308
Cdd:PRK13837  529 IAPLLR-VSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDISLSRAklrapkvlshgvlppGRY 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 309 SQIEVADEGEGIDSDIMPHIFDRFrqadsSTRRShGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSAVVA 388
Cdd:PRK13837  608 VLLRVSDTGAGIDEAVLPHIFEPF-----FTTRA-GGTGLGLATVHGIVSAHAGYIDVQS-TVGRGTRFDVYLPPSSKVP 680

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 389 EGhaqrPDTSAPRAAAPRSeidlSGVRVLVVDDEPDGR---EAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDI 465
Cdd:PRK13837  681 VA----PQAFFGPGPLPRG----RGETVLLVEPDDATLeryEEKLAALGYEPVGFSTLAAAIAWISKGPERFDLVLVDDR 752

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758 466 GMPEEdgyDLIRRVRDLAPAEGGRVPAMALTAFAREEDRLRAIEAgfqvhAIKPVQPAELAAGVA 530
Cdd:PRK13837  753 LLDEE---QAAAALHAAAPTLPIILGGNSKTMALSPDLLASVAEI-----LAKPISSRTLAYALR 809

REC_OmpR

cd17574

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...

417-511

5.65e-22

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 90.54 E-value: 5.65e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 417 LVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMALT 496
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLR----EKGSDIPIIMLT 76

                          90
                  ....*....|....*
gi 1232315758 497 AFAREEDRLRAIEAG 511
Cdd:cd17574    77 AKDEEEDKVLGLELG 91

KinA

COG5805

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...

166-384

1.91e-21

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: 97.49 E-value: 1.91e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 166 ATLSHELRTPLTAMLGWTQLLRSGALTADEEVRgleiIERNVLAQAKLI-DDLLDVSRIVTgklrLNVRPLSLASVIEAA 244
Cdd:COG5805   292 AGIAHEIRNPLTSIKGFLQLLQPGIEDKEEYFD----IMLSELDRIESIiSEFLALAKPQA----VNKEKENINELIQDV 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 245 LDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDI 324
Cdd:COG5805   364 VTLLETEAILHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEER 443

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 325 MPHIFDRFrqadSSTRRShgGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLS 384
Cdd:COG5805   444 LKKLGEPF----FTTKEK--GTGLGLMVSYKIIENHNGTIDIDS-KVGKGTTFTITLPLS 496

marine_sort_HK

TIGR03785

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...

121-382

2.78e-21

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.

Pssm-ID: 163497 [Multi-domain] Cd Length: 703 Bit Score: 97.89 E-value: 2.78e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 121 GKCQGDF---TSEDEavLLQLAQMASIAIentlnSEAREANRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEV 197
Cdd:TIGR03785 449 GRISGAIpasRSRDE--IGDLSRSFAQMV-----ARLRQYTHYLENMSSRLSHELRTPVAVVRSSLENLELQALEQEKQK 521

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 198 ---RGLEIIERnvlaQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAadAKAVRFEPLLDERAGHVTGDP 274
Cdd:TIGR03785 522 yleRAREGTER----LSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGCMQGYQMT--YPPQRFELNIPETPLVMRGSP 595

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 275 DRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVR 354
Cdd:TIGR03785 596 ELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKSHALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYIVR 675

                         250       260
                  ....*....|....*....|....*...
gi 1232315758 355 HVVELHGGSVRAESLGAGHGATFVVELP 382
Cdd:TIGR03785 676 LIADFHQGRIQAENRQQNDGVVFRISLP 703

HATPase_CpxA-like

cd16949

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-383

1.67e-20

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: 86.61 E-value: 1.67e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPvgGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHV 356
Cdd:cd16949     1 LARALENVLRNALRYSP--SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERA 78

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 357 VELHGGSVRAESlGAGHGATFVVELPL 383
Cdd:cd16949    79 IEQHGGKIKASN-RKPGGLRVRIWLPA 104

REC_NarL-like

cd17535

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...

416-529

7.97e-20

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381090 [Multi-domain] Cd Length: 117 Bit Score: 85.26 E-value: 7.97e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYH--AQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAM 493
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPdiEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP----DLKVI 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd17535    77 VLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112

HATPase_AtoS-like

cd16943

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

274-383

8.11e-20

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: 84.78 E-value: 8.11e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 274 PDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRSHGGLGLGLAIV 353
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPF----FTTKPVGEGTGLGLSLS 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 354 RHVVELHGGSVRAESLgAGHGATFVVELPL 383
Cdd:cd16943    77 YRIIQKHGGTIRVASV-PGGGTRFTIILPI 105

CitB

COG4565

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...

415-535

1.73e-19

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];

Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 85.02 E-value: 1.73e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVY--HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPA 492
Cdd:COG4565     5 RVLIVEDDPMVAELLRRYLERLpgFEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELR----ARGPDVDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:COG4565    81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEY 123

REC_D1_PleD-like

cd17538

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...

415-511

2.83e-19

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381093 [Multi-domain] Cd Length: 104 Bit Score: 82.93 E-value: 2.83e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPAMA 494
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLK--EDPETRHIPVIM 78

                          90
                  ....*....|....*..
gi 1232315758 495 LTAFAREEDRLRAIEAG 511
Cdd:cd17538    79 ITALDDREDRIRGLEAG 95

REC_DivK-like

cd17548

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...

415-531

2.98e-19

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381100 [Multi-domain] Cd Length: 115 Bit Score: 83.36 E-value: 2.98e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPAMA 494
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLK--EDPATRDIPVIA 78

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:cd17548    79 LTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115

REC_HupR-like

cd17569

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...

415-525

3.01e-19

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381113 [Multi-domain] Cd Length: 118 Bit Score: 83.61 E-value: 3.01e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaEGGRvpaMA 494
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYP-DTVR---IL 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGfQVHAI--KPVQPAEL 525
Cdd:cd17569    78 LTGYADLDAAIEAINEG-EIYRFltKPWDDEEL 109

HATPase_BasS-like

cd16940

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

270-381

4.33e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.

Pssm-ID: 340417 [Multi-domain] Cd Length: 113 Bit Score: 82.84 E-value: 4.33e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 270 VTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSrSQIEVADEGEGIDSDIMPHIFDRFRQADSstrRSHGGLGLG 349
Cdd:cd16940     7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDG-AVIRVEDNGPGIDEEELEALFERFYRSDG---QNYGGSGLG 82

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 350 LAIVRHVVELHGGSVRaesLGAGHGATFVVEL 381
Cdd:cd16940    83 LSIVKRIVELHGGQIF---LGNAQGGGLEAWV 111

REC_RpfG-like

cd17551

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...

415-527

5.74e-19

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381103 [Multi-domain] Cd Length: 118 Bit Score: 82.49 E-value: 5.74e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVL-SVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapAEGGRVPAM 493
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLrSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRAL--PGLEDVPIV 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 494 ALTAFAREEDRLRAIEAGfqvhAI----KPVQPAELAA 527
Cdd:cd17551    80 MITADTDREVRLRALEAG----ATdfltKPFDPVELLA 113

CitA

COG3290

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...

165-384

7.67e-19

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

Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 88.75 E-value: 7.67e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 165 LATLSHELRTPLTAMLGWTQLLRsgaltaDEEVRgleiiernvlaqaKLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAA 244
Cdd:COG3290   193 LRAQRHDFRNHLHTISGLLQLGE------YDEAL-------------EYIDEISEELQELIDSLLSRIGNPVLAALLLGK 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 245 LDVvrpaADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAV----KFSPVGGKIRVSLTRQGSRSQIEVADEGEGI 320
Cdd:COG3290   254 AAR----ARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERRVELSIRDDGDELVIEVEDSGPGI 329

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1232315758 321 DSDIMPHIFDRfrqaDSSTRRSHGGlGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLS 384
Cdd:COG3290   330 PEELLEKIFER----GFSTKLGEGR-GLGLALVKQIVEKYGGTIEVES-EEGEGTVFTVRLPKE 387

HATPase_VanS-like

cd16923

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

1.11e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.

Pssm-ID: 340400 [Multi-domain] Cd Length: 102 Bit Score: 81.28 E-value: 1.11e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHV 356
Cdd:cd16923     1 LQRVFSNLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAI 78

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 357 VELHGGSVRAESlgAGHGATFVVELP 382
Cdd:cd16923    79 IELHGGSASAEY--DDNHDLFKVRLP 102

LytT

COG3279

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...

415-532

2.22e-18

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];

Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 84.48 E-value: 2.22e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVY--HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPA 492
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYpdLEVVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP----PPPI 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1232315758 493 MALTAFAReedrlRAIEAgFQVHAI----KPVQPAELAAGVAKL 532
Cdd:COG3279    79 IFTTAYDE-----YALEA-FEVNAVdyllKPIDEERLAKALEKA 116

REC_YesN-like

cd17536

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...

416-535

2.85e-18

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381091 [Multi-domain] Cd Length: 121 Bit Score: 80.84 E-value: 2.85e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVL--SVYHAQ-VATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPA 492
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYP----DIKI 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1232315758 493 MALTAF-----AREedrlrAIEAGfqVHA--IKPVQPAELAAGVAKLAGR 535
Cdd:cd17536    77 IILSGYddfeyAQK-----AIRLG--VVDylLKPVDEEELEEALEKAKEE 119

HATPase_RstB-like

cd16939

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-383

6.28e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.

Pssm-ID: 340416 [Multi-domain] Cd Length: 104 Bit Score: 79.40 E-value: 6.28e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSpvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHV 356
Cdd:cd16939     1 MARALDNLLRNALRYA--HRTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRV 78

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 357 VELHGGSVRAESLGAGhGATFVVELPL 383
Cdd:cd16939    79 ALWHGGHVECDDSELG-GACFRLTWPR 104

REC_OmpR_PhoB

cd17618

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...

415-527

6.29e-18

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381133 [Multi-domain] Cd Length: 118 Bit Score: 79.60 E-value: 6.29e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPAMA 494
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLK--RDEMTRDIPIIM 79

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17618    80 LTARGEEEDKVRGLEAGADDYITKPFSPRELVA 112

PRK10337

sensor protein QseC; Provisional

164-365

1.34e-17

sensor protein QseC; Provisional

Pssm-ID: 182388 [Multi-domain] Cd Length: 449 Bit Score: 85.47 E-value: 1.34e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 164 FLATLSHELRTPLTAMLGWTQLLRsgaLTADEEV---RGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASV 240
Cdd:PRK10337  240 FTSDAAHELRSPLAALKVQTEVAQ---LSDDDPQarkKALLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDL 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 241 IEAALDVVRPAADAKAVrfEPLLDERAGHV--TGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGsrsqIEVADEGE 318
Cdd:PRK10337  317 LQSAVMDIYHTAQQAGI--DVRLTLNAHPVirTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNARN----FTVRDNGP 390

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1232315758 319 GIDSDIMPHIFDRFRQADSSTRrshGGLGLGLAIVRHVVELHGGSVR 365
Cdd:PRK10337  391 GVTPEALARIGERFYRPPGQEA---TGSGLGLSIVRRIAKLHGMNVS 434

PRK10755

two-component system sensor histidine kinase PmrB;

145-382

1.43e-17

two-component system sensor histidine kinase PmrB;

Pssm-ID: 236751 [Multi-domain] Cd Length: 356 Bit Score: 84.25 E-value: 1.43e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 145 AIENTLNS-EAREANRIKDE--FLATLSHELRTPLTAmlgwtqllrsgaltadeeVR-GLEIIERNVLAQA--------- 211
Cdd:PRK10755  118 AVTSALNQlVSRLTSTLDQErlFTADVAHELRTPLAG------------------IRlHLELLEKQHHIDVapliarldq 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 212 --KLIDDLLDVSRI----VTGklrlNVRPLSLAS-VIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNL 284
Cdd:PRK10755  180 mmHTVEQLLQLARAgqsfSSG----HYQTVKLLEdVILPSQDELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 285 LVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSstrrSHGGLGLGLAIVRHVVELHGGSV 364
Cdd:PRK10755  256 VENAHRYSPEGSTITIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHGQF 331

                         250
                  ....*....|....*...
gi 1232315758 365 RAESLGAGHGATFVVELP 382
Cdd:PRK10755  332 FLQNRQERSGTRAWVWLP 349

HATPase_EcPhoR-like

cd16952

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

2.52e-17

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

Pssm-ID: 340428 [Multi-domain] Cd Length: 108 Bit Score: 77.63 E-value: 2.52e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHV 356
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHV 80

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 357 VELHGGSVRAESLgAGHGATFVVELP 382
Cdd:cd16952    81 MSRHDARLLIASE-LGKGSRFTCLFP 105

cpxA

PRK09470

envelope stress sensor histidine kinase CpxA;

140-384

2.95e-17

envelope stress sensor histidine kinase CpxA;

Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 84.60 E-value: 2.95e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 140 QMASiAIENTLNSEAReanrikdeFLATLSHELRTPLTAMLGWTQLL--RSGaltadeEVRGLEIIERNVLAQAKLIDDL 217
Cdd:PRK09470  231 QMVT-ALERMMTSQQR--------LLSDISHELRTPLTRLQLATALLrrRQG------ESKELERIETEAQRLDSMINDL 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 218 LDVSRIVTgKLRLNVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSpvGGK 297
Cdd:PRK09470  296 LVLSRNQQ-KNHLERETFKANSLWSEVLEDAKFEAEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNALRYS--HTK 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 298 IRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAES--LGaghGA 375
Cdd:PRK09470  373 IEVAFSVDKDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAEDspLG---GL 449


                  ....*....
gi 1232315758 376 TFVVELPLS 384
Cdd:PRK09470  450 RLTIWLPLY 458

REC_OmpR_KdpE-like

cd17620

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...

416-511

6.67e-17

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381135 [Multi-domain] Cd Length: 99 Bit Score: 76.05 E-value: 6.67e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMAL 495
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR-----EWSAVPVIVL 75

                          90
                  ....*....|....*.
gi 1232315758 496 TAFAREEDRLRAIEAG 511
Cdd:cd17620    76 SARDEESDKIAALDAG 91

HATPase_FilI-like

cd16921

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

6.82e-17

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: 76.21 E-value: 6.82e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFS--PVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSstRRSHGGLGLGLAIVR 354
Cdd:cd16921     1 LGQVLTNLLGNAIKFRrpRRPPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHS--REEYEGTGVGLAIVR 78

                          90       100
                  ....*....|....*....|....*...
gi 1232315758 355 HVVELHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16921    79 KIIERHGGRIWLES-EPGEGTTFYFTLP 105

REC_OmpR_MtPhoP-like

cd17615

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...

415-527

7.54e-17

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381131 [Multi-domain] Cd Length: 118 Bit Score: 76.62 E-value: 7.54e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMA 494
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLR----ADGPDVPVLF 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17615    77 LTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVA 109

HATPase_BvrS-ChvG-like

cd16953

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

1.46e-16

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

Pssm-ID: 340429 [Multi-domain] Cd Length: 110 Bit Score: 75.69 E-value: 1.46e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSP-VGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRH 355
Cdd:cd16953     1 LGQVLRNLIGNAISFSPpDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQ 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 356 VVELHGGSVRAESL---GAGHGATFVVELP 382
Cdd:cd16953    81 IIEAHGGISVAENHnqpGQVIGARFTVQLP 110

HisKA

cd00082

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...

158-222

1.76e-16

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.

Pssm-ID: 119399 [Multi-domain] Cd Length: 65 Bit Score: 73.79 E-value: 1.76e-16

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758 158 NRIKDEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLEIIERNVLAQAKLIDDLLDVSR 222
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65

REC_RR468-like

cd17552

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...

415-534

2.60e-16

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381104 [Multi-domain] Cd Length: 121 Bit Score: 75.28 E-value: 2.60e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHA-QVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPAM 493
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQ--ANPETQSIPVI 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1232315758 494 ALTAFAREEDRLRAIEAGfqVHAI--KPVQPAELAAGVAKLAG 534
Cdd:cd17552    81 LLTAKAQPSDRQRFASLG--VAGViaKPFDPLTLAEQIAKLLG 121

HATPase_TmoS-FixL-DctS-like

cd16920

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

2.64e-16

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

Pssm-ID: 340397 [Multi-domain] Cd Length: 104 Bit Score: 74.74 E-value: 2.64e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVK----FSPVGGKIRVSLTRQGSRS-QIEVADEGEGIDSDIMPHIFDRFRQADSStrrshgGLGLGLA 351
Cdd:cd16920     1 IQQVLINLVRNGIEamseGGCERRELTIRTSPADDRAvTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGLS 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 352 IVRHVVELHGGSVRAESLGAGhGATFVVELP 382
Cdd:cd16920    75 ICRSIIEAHGGRLSVESPAGG-GATFQFTLP 104

REC_PA4781-like

cd19920

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...

416-511

2.90e-16

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381147 [Multi-domain] Cd Length: 103 Bit Score: 74.47 E-value: 2.90e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVR-DLAPAEggrVPAMA 494
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKaDPATRH---IPVIF 77

                          90
                  ....*....|....*..
gi 1232315758 495 LTAFAREEDRLRAIEAG 511
Cdd:cd19920    78 LTALTDTEDKVKGFELG 94

PRK11361

acetoacetate metabolism transcriptional regulator AtoC;

415-525

4.25e-16

acetoacetate metabolism transcriptional regulator AtoC;

Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 80.66 E-value: 4.25e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMA 494
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET----RTPVIL 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:PRK11361   82 MTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112

HATPase_CreC-like

cd16945

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

273-376

1.41e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.

Pssm-ID: 340421 [Multi-domain] Cd Length: 106 Bit Score: 72.49 E-value: 1.41e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRSHGG---LGLG 349
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERF----YSLPRPHSGqksTGLG 76

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 350 LAIVRHVVELHGGSVRAESLGAGHGAT 376
Cdd:cd16945    77 LAFVQEVAQLHGGRITLRNRPDGVLAF 103

REC_hyHK

cd17598

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...

416-519

1.58e-15

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 72.74 E-value: 1.58e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVR---DLApaeggRVPA 492
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKsdpDLK-----DIPV 75

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd17598    76 ILLTTLSDPRDVIRGLECGADNFITKP 102

orf27

CHL00148

Ycf27; Reviewed

415-527

2.34e-15

Ycf27; Reviewed

Pssm-ID: 214376 [Multi-domain] Cd Length: 240 Bit Score: 75.91 E-value: 2.34e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDL---IRRVRDlapaeggrVP 491
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVcqeIRKESD--------VP 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232315758 492 AMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:CHL00148   80 IIMLTALGDVSDRITGLELGADDYVVKPFSPKELEA 115

REC_OmpR_PrrA-like

cd17627

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...

416-535

2.73e-15

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381142 [Multi-domain] Cd Length: 116 Bit Score: 72.03 E-value: 2.73e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR----AAGNDLPILVL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:cd17627    77 TARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALLRR 116

HisKA

smart00388

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...

161-226

3.34e-15

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.

Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 70.29 E-value: 3.34e-15

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758  161 KDEFLATLSHELRTPLTAMLGWTQLLRSGALTaDEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTG 226
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELS-EEQREYLETILREAERLLRLINDLLDLSRIEAG 66

HATPase_EnvZ-like

cd16950

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

3.95e-15

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

Pssm-ID: 340426 [Multi-domain] Cd Length: 101 Bit Score: 71.33 E-value: 3.95e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSpvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHV 356
Cdd:cd16950     1 LKRVLSNLVDNALRYG--GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRI 76

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 357 VELHGGSVRAESLGAGhGATFVVELP 382
Cdd:cd16950    77 SDAHGGSLTLANRAGG-GLCARIELP 101

REC_OmpR_BsPhoP-like

cd19937

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...

417-529

4.92e-15

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381164 [Multi-domain] Cd Length: 116 Bit Score: 71.54 E-value: 4.92e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 417 LVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPAMALT 496
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILR--SDPKTSSIPIIMLT 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 497 AFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd19937    79 AKGEEFDKVLGLELGADDYITKPFSPRELLARV 111

REC_RssB-like

cd17555

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...

414-521

6.47e-15

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381107 [Multi-domain] Cd Length: 116 Bit Score: 71.08 E-value: 6.47e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAM 493
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESP----DTPVI 76

                          90       100
                  ....*....|....*....|....*...
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQ 521
Cdd:cd17555    77 VVSGAGVMSDAVEALRLGAWDYLTKPIE 104

envZ

PRK09467

osmolarity sensor protein; Provisional

165-365

1.29e-14

osmolarity sensor protein; Provisional

Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 76.10 E-value: 1.29e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 165 LATLSHELRTPLT-------AMLGWTQLLRSGALTADEEVRglEIIErnvlaqaKLIDDLLDVSRIVTGKLRLNvrplsl 237
Cdd:PRK09467  233 MAGVSHDLRTPLTrirlateMMSEEDGYLAESINKDIEECN--AIIE-------QFIDYLRTGQEMPMEMADLN------ 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 238 aSVIEaalDVVRPAADAKAVrFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSpvGGKIRVSLTRQGSRSQIEVADEG 317
Cdd:PRK09467  298 -ALLG---EVIAAESGYERE-IETALQPGPIEVPMNPIAIKRALANLVVNAARYG--NGWIKVSSGTEGKRAWFQVEDDG 370

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1232315758 318 EGIDSDIMPHIFDRFRQADSStrRSHGGLGLGLAIVRHVVELHGGSVR 365
Cdd:PRK09467  371 PGIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKVE 416

REC_LytTR_AlgR-like

cd17532

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...

416-533

1.58e-14

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381087 [Multi-domain] Cd Length: 118 Bit Score: 69.87 E-value: 1.58e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSvYHAQ---VATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRVPA 492
Cdd:cd17532     1 ALIVDDEPLAREELRYLLE-EHPDieiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLA-----KPPL 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1232315758 493 MA-LTAFareedRLRAIEAgFQVHAI----KPVQPAELAAGVAKLA 533
Cdd:cd17532    75 IVfVTAY-----DEYAVEA-FELNAVdyllKPFSEERLAEALAKLR 114

REC_2_GGDEF

cd17544

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...

414-480

1.71e-14

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381098 [Multi-domain] Cd Length: 122 Bit Score: 69.86 E-value: 1.71e-14

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQaRPDV--LISDIGMPEEDGYDLIRRVR 480
Cdd:cd17544     1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ-HPDIklVITDYNMPEMDGFELVREIR 68

HisKA

pfam00512

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...

161-226

2.19e-14

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.

Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 68.01 E-value: 2.19e-14

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1232315758 161 KDEFLATLSHELRTPLTAMLGWTQLLRSGALTaDEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTG 226
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLD-EEQREYLETILRSAERLLRLINDLLDLSRIEAG 66

AmiR

COG3707

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...

413-530

2.62e-14

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];

Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 71.53 E-value: 2.62e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 413 GVRVLVVDDEPDGREAIAKVLSVY-HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrvP 491
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERPA-----P 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315758 492 AMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVA 530
Cdd:COG3707    78 VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116

HATPase_DpiB-CitA-like

cd16915

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

280-382

3.91e-14

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: 68.47 E-value: 3.91e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 280 VVWNLLVNAVKFS----PVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRfrqadSSTRRSHGGLGLGLAIVRH 355
Cdd:cd16915     4 IVGNLIDNALDALaatgAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQ 78

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 356 VVELHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16915    79 SVERLGGSITVES-EPGGGTTFSIRIP 104

PRK11083

DNA-binding response regulator CreB; Provisional

415-542

5.07e-14

DNA-binding response regulator CreB; Provisional

Pssm-ID: 236838 [Multi-domain] Cd Length: 228 Bit Score: 71.53 E-value: 5.07e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMA 494
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPA----LPVIF 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPSGP 542
Cdd:PRK11083   81 LTARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTILRRVKKFAAP 128

REC_TrrA-like

cd17554

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...

415-498

6.01e-14

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381106 [Multi-domain] Cd Length: 113 Bit Score: 68.02 E-value: 6.01e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMA 494
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKP----DLPVII 77


                  ....
gi 1232315758 495 LTAF 498
Cdd:cd17554    78 CTAY 81

HATPase_HupT_MifS-like

cd16976

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-381

6.78e-14

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: 67.87 E-value: 6.78e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAvkFSPVGG----KIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRSHGGLGLGLAI 352
Cdd:cd16976     1 IQQVLMNLLQNA--LDAMGKvenpRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPF----FTTKPVGKGTGLGLSI 74

                          90       100
                  ....*....|....*....|....*....
gi 1232315758 353 VRHVVELHGGSVRAESLGAGhGATFVVEL 381
Cdd:cd16976    75 SYGIVEEHGGRLSVANEEGA-GARFTFDL 102

REC_Ycf29

cd19927

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...

416-519

8.78e-14

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381154 [Multi-domain] Cd Length: 102 Bit Score: 67.40 E-value: 8.78e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDlaPAEGGRVPAMAL 495
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRK--NADFDTIPVIFL 78

                          90       100
                  ....*....|....*....|....
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd19927    79 TAKGMTSDRIKGYNAGCDGYLSKP 102

REC_DctD-like

cd17549

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...

416-484

1.08e-13

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381101 [Multi-domain] Cd Length: 130 Bit Score: 67.90 E-value: 1.08e-13

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDP 69

REC_NtrX-like

cd17550

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...

416-484

1.10e-13

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381102 [Multi-domain] Cd Length: 115 Bit Score: 67.52 E-value: 1.10e-13

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYP 69

REC_OmpR_DrrD-like

cd17625

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...

417-535

2.44e-13

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381140 [Multi-domain] Cd Length: 115 Bit Score: 66.48 E-value: 2.44e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 417 LVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMALT 496
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLR----EEGIETPVLLLT 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315758 497 AFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:cd17625    77 ALDAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115

REC_CheB-like

cd17541

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...

414-511

2.53e-13

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381096 [Multi-domain] Cd Length: 125 Bit Score: 66.65 E-value: 2.53e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLS------VyhaqVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeg 487
Cdd:cd17541     1 IRVLIVDDSAVMRKLLSRILEsdpdieV----VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP--- 73

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 488 grVPAMALTAFAREEDR--LRAIEAG 511
Cdd:cd17541    74 --TPVVMVSSLTEEGAEitLEALELG 97

HATPase_YcbM-like

cd16947

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

263-368

4.30e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).

Pssm-ID: 340423 [Multi-domain] Cd Length: 125 Bit Score: 66.00 E-value: 4.30e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 263 LDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTRRS 342
Cdd:cd16947     7 IPDRPIYANANTEALQRILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSA 86

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 343 HGGLGLGLAIVRHVVELHGGSVRAES 368
Cdd:cd16947    87 KQGNGLGLTITKRLAESMGGSIYVNS 112

REC_CheY_CheY3

cd19923

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...

414-532

5.12e-13

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 65.82 E-value: 5.12e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLS-VYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPA 492
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKeLGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIR--ADGALSHLPV 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:cd19923    79 LMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKI 118

CitB

COG2197

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...

414-517

9.05e-13

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];

Pssm-ID: 441799 [Multi-domain] Cd Length: 131 Bit Score: 65.30 E-value: 9.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYH--AQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVrdlapaeggrvp 491
Cdd:COG2197     2 IRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL------------ 69

                          90       100
                  ....*....|....*....|....*.
gi 1232315758 492 amaLTafAREEDRLRAIEAGFQVHAI 517
Cdd:COG2197    70 ---LT--PREREVLRLLAEGLSNKEI 90

REC_OmpR_EcPhoP-like

cd19934

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...

416-527

1.04e-12

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381161 [Multi-domain] Cd Length: 117 Bit Score: 64.61 E-value: 1.04e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWR----SEGRATPVLIL 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd19934    77 TARDSWQDKVEGLDAGADDYLTKPFHIEELLA 108

REC_CheY

cd17542

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...

414-532

1.10e-12

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381097 [Multi-domain] Cd Length: 117 Bit Score: 64.61 E-value: 1.10e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSV--YHAqVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeGGRVp 491
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKagYEV-VGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDP--NAKV- 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 492 aMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:cd17542    77 -IMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116

REC_HupR

cd17596

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...

415-526

1.33e-12

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381127 [Multi-domain] Cd Length: 133 Bit Score: 65.08 E-value: 1.33e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVyHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMA 494
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPE----VVRII 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAI-EAGFQVHAIKPVQPAELA 526
Cdd:cd17596    77 ISGYTDSEDIIAGInEAGIYQYLTKPWHPDQLL 109

HATPase_Glnl-NtrB-like

cd16918

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-382

1.38e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).

Pssm-ID: 340395 [Multi-domain] Cd Length: 109 Bit Score: 64.34 E-value: 1.38e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVK-FSPVGGKIR--------VSLTRQGSR--SQIEVADEGEGIDSDIMPHIFDRFrqadSSTRRshGG 345
Cdd:cd16918     1 LIQVFLNLVRNAAQaLAGSGGEIIlrtrtqrqVTLGHPRHRlaLRVSVIDNGPGIPPDLQDTIFYPM----VSGRE--NG 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1232315758 346 LGLGLAIVRHVVELHGGSVRAESlGAGHgATFVVELP 382
Cdd:cd16918    75 TGLGLAIAQNIVSQHGGVIECDS-QPGH-TVFSVSLP 109

COG4192

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...

105-382

1.65e-12

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];

Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 70.10 E-value: 1.65e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 105 PLTGRD--GRDMGLLHVcgkcqgdFTSEDEAVLLQLAQMAS--IAIENtlNSEAREANRIKDEFLA-------TLSHELR 173
Cdd:COG4192   375 PVDGNDeiGRIARLLRV-------FRDQAIEKTQELETEIEerKRIEK--NLRQTQDELIQAAKMAvvgqtmtSLAHELN 445

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 174 TPLTAMLGW-----TQLLRSGALTADEEvrgLEIIERNVLAQAKLIDDLLDVSRIVTGKLRlnvrPLSLASVIEAALDVV 248
Cdd:COG4192   446 QPLNAMSMYlfsakKALEQENYAQLPTS---LDKIEGLIERMDKIIKSLRQFSRKSDTPLQ----PVDLRQVIEQAWELV 518

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 249 RPAADAKAVRFEPLLDERaghVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIdsDIMPHI 328
Cdd:COG4192   519 ESRAKPQQITLHIPDDLM---VQGDQVLLEQVLVNLLVNALDAVATQPQISVDLLSNAENLRVAISDNGNGW--PLVDKL 593

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758 329 FDRFrqadSSTRRShgGLGLGLAIVRHVVELHGGSVR-AESLgaGHGATFVVELP 382
Cdd:COG4192   594 FTPF----TTTKEV--GLGLGLSICRSIMQQFGGDLYlASTL--ERGAMVILEFN 640

REC_OmpR_CusR-like

cd19935

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...

416-511

2.77e-12

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381162 [Multi-domain] Cd Length: 100 Bit Score: 62.84 E-value: 2.77e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLR----AAGKQTPVLML 76

                          90
                  ....*....|....*.
gi 1232315758 496 TAFAREEDRLRAIEAG 511
Cdd:cd19935    77 TARDSVEDRVKGLDLG 92

REC_CheY4-like

cd17562

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...

415-532

3.37e-12

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381110 [Multi-domain] Cd Length: 118 Bit Score: 63.47 E-value: 3.37e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEGgrVPAMA 494
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKF--TPILM 79

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:cd17562    80 LTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKV 117

REC_PdtaR-like

cd19932

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...

414-525

4.25e-12

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381159 [Multi-domain] Cd Length: 118 Bit Score: 63.20 E-value: 4.25e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVL-SVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrvPA 492
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLeEAGYEVVGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSENIA-----PI 75

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd19932    76 VLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108

REC_OmpR_ArcA_TorR-like

cd17619

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...

415-525

6.02e-12

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381134 [Multi-domain] Cd Length: 113 Bit Score: 62.40 E-value: 6.02e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMA 494
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR-----EQSEVGIIL 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17619    77 VTGRDDEVDRIVGLEIGADDYVTKPFNPREL 107

HATPase_BceS-YxdK-YvcQ-like

cd16948

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

284-382

9.67e-12

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: 61.92 E-value: 9.67e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 284 LLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRF------RQADSSTrrshgglGLGLAIVRHVV 357
Cdd:cd16948    13 IVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgengRNFQEST-------GMGLYLVKKLC 85

                          90       100
                  ....*....|....*....|....*
gi 1232315758 358 ELHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16948    86 DKLGHKIDVES-EVGEGTTFTITFP 109

REC_NtrC

cd19919

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...

415-523

9.69e-12

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381146 [Multi-domain] Cd Length: 116 Bit Score: 61.91 E-value: 9.69e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMA 494
Cdd:cd19919     2 TVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHP----DLPVII 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 495 LTAFAREEDRLRAIEAG--------FQV-HAIKPVQPA 523
Cdd:cd19919    78 MTAHSDLDSAVSAYQGGafeylpkpFDIdEAVALVERA 115

PRK10816

two-component system response regulator PhoP;

415-536

1.18e-11

two-component system response regulator PhoP;

Pssm-ID: 182755 [Multi-domain] Cd Length: 223 Bit Score: 64.37 E-value: 1.18e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMA 494
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWR----SNDVSLPILV 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRD 536
Cdd:PRK10816   78 LTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRN 119

pleD

PRK09581

response regulator PleD; Reviewed

415-532

1.35e-11

response regulator PleD; Reviewed

Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 66.85 E-value: 1.35e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAI-AKVLSVYHaQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVR-DLAPAEggrVPA 492
Cdd:PRK09581    4 RILVVDDIPANVKLLeAKLLAEYY-TVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKsDPATTH---IPV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:PRK09581   80 VMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSL 119

REC_OmpR_MtrA-like

cd17626

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...

415-529

1.55e-11

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381141 [Multi-domain] Cd Length: 115 Bit Score: 61.33 E-value: 1.55e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGrVPAMA 494
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR----AESG-VPIVM 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd17626    77 LTAKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111

COG4567

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...

415-540

1.83e-11

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];

Pssm-ID: 443624 [Multi-domain] Cd Length: 177 Bit Score: 63.01 E-value: 1.83e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMA 494
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPD----ARIVV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPS 540
Cdd:COG4567    82 LTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPP 127

REC

smart00448

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...

415-468

1.93e-11

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.

Pssm-ID: 214668 [Multi-domain] Cd Length: 55 Bit Score: 59.12 E-value: 1.93e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1232315758  415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMP 468
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

REC_CheV-like

cd19924

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...

416-511

1.94e-11

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381151 [Multi-domain] Cd Length: 111 Bit Score: 60.86 E-value: 1.94e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARP---------DVLISDIGMPEEDGYDLIRRVRD---LA 483
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDdprLA 80

                          90       100
                  ....*....|....*....|....*...
gi 1232315758 484 paeggRVPAMALTAFAREEDRLRAIEAG 511
Cdd:cd19924    81 -----NIPVILNSSLSGEFSRARGKKVG 103

REC_OmpR_BaeR-like

cd19938

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...

415-529

2.75e-11

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381165 [Multi-domain] Cd Length: 114 Bit Score: 60.47 E-value: 2.75e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDgreaIAKVLSVYHAQVATASS----AREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRV 490
Cdd:cd19938     1 RILIVEDEPK----LAQLLIDYLRAAGYAPTllahGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-----DV 71

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315758 491 PAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd19938    72 PIIMVTARVEEIDRLLGLELGADDYICKPYSPREVVARV 110

REC_typeB_ARR-like

cd17584

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...

416-527

3.65e-11

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381121 [Multi-domain] Cd Length: 115 Bit Score: 60.33 E-value: 3.65e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARP--DVLISDIGMPEEDGYDLIRRVRDLApaeggRVPAM 493
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDefDLVITDVHMPDMDGFEFLELIRLEM-----DLPVI 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17584    76 MMSADGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109

HATPase_SpaK_NisK-like

cd16975

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

273-380

4.01e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.

Pssm-ID: 340434 [Multi-domain] Cd Length: 107 Bit Score: 60.17 E-value: 4.01e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStRRSHGGLGLGLAI 352
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTS-RRSGGHYGMGLYI 79

                          90       100
                  ....*....|....*....|....*...
gi 1232315758 353 VRHVVELHGGSVRAESLGAGhGATFVVE 380
Cdd:cd16975    80 AKNLVEKHGGSLIIENSQKG-GAEVTVK 106

REC_OmpR_PmrA-like

cd17624

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...

416-527

5.24e-11

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381139 [Multi-domain] Cd Length: 115 Bit Score: 59.81 E-value: 5.24e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWR----RQGQSLPVLIL 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17624    77 TARDGVDDRVAGLDAGADDYLVKPFALEELLA 108

HATPase_PhoQ-like

cd16954

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

272-381

5.24e-11

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.

Pssm-ID: 340430 [Multi-domain] Cd Length: 135 Bit Score: 60.34 E-value: 5.24e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 272 GDPDRLQQVVWNLLVNAVKFSpvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSStrrsHGGLGLGLA 351
Cdd:cd16954    33 GERNDLMELLGNLLDNACKWC--LEFVEVTARQTDGGLHLIVDDDGPGVPESQRSKIFQRGQRLDEQ----RPGQGLGLA 106

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 352 IVRHVVELHGGSVRAESLGAGhGATFVVEL 381
Cdd:cd16954   107 IAKEIVEQYGGELSLSDSPLG-GARFEVVF 135

REC_Rcp-like

cd17557

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...

415-525

8.75e-11

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381108 [Multi-domain] Cd Length: 129 Bit Score: 59.74 E-value: 8.75e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVL--SVYHAQVATASSAREALAL------FAQA-RPDVLISDIGMPEEDGYDLIRRVR---DL 482
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFkeAGVPNELHVVRDGEEALDFlrgegeYADApRPDLILLDLNMPRMDGFEVLREIKadpDL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1232315758 483 ApaeggRVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17557    81 R-----RIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEF 118

REC_OmpR_YycF-like

cd17614

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...

416-529

8.92e-11

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381130 [Multi-domain] Cd Length: 115 Bit Score: 59.36 E-value: 8.92e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMAL 495
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR-----KTSNVPIIML 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd17614    76 TAKDSEVDKVLGLELGADDYVTKPFSNRELLARV 109

REC_OmpR_kpRstA-like

cd17622

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...

415-527

1.27e-10

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381137 [Multi-domain] Cd Length: 116 Bit Score: 58.93 E-value: 1.27e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrvPAMA 494
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-----PILL 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17622    77 LTALDSDIDHILGLELGADDYVVKPVEPAVLLA 109

FixJ

COG4566

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...

416-537

1.97e-10

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];

Pssm-ID: 443623 [Multi-domain] Cd Length: 196 Bit Score: 60.50 E-value: 1.97e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELA----ARGSPLPVIFL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1232315758 496 TAFAREEDRLRAIEAGfqvhAI----KPVQPAELAAGVAKLAGRDA 537
Cdd:COG4566    78 TGHGDVPMAVRAMKAG----AVdfleKPFDDQALLDAVRRALARDR 119

REC_OmpR_CpxR

cd17623

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...

416-527

2.07e-10

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381138 [Multi-domain] Cd Length: 115 Bit Score: 58.09 E-value: 2.07e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMAL 495
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR-----KTSQVPVLML 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17623    76 TARGDDIDRILGLELGADDYLPKPFNPRELVA 107

REC_CpdR_CckA-like

cd18160

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...

415-502

2.54e-10

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381144 [Multi-domain] Cd Length: 103 Bit Score: 57.51 E-value: 2.54e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARP-DVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAM 493
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPD----VKIL 76


                  ....*....
gi 1232315758 494 ALTAFAREE 502
Cdd:cd18160    77 FISGGAAAA 85

PRK10161

phosphate response regulator transcription factor PhoB;

415-539

2.85e-10

phosphate response regulator transcription factor PhoB;

Pssm-ID: 182277 [Multi-domain] Cd Length: 229 Bit Score: 60.50 E-value: 2.85e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEGgrVPAMA 494
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRD--IPVVM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVaKLAGRDASP 539
Cdd:PRK10161   82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARI-KAVMRRISP 125

REC_citrate_TCS

cd19925

phosphoacceptor receiver (REC) domain of citrate family two-component system response ...

414-527

7.28e-10

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381152 [Multi-domain] Cd Length: 118 Bit Score: 56.87 E-value: 7.28e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPdgreAIAKVLSVYHAQV------ATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEG 487
Cdd:cd19925     1 INVLIVEDDP----MVAEIHRAYVEQVpgftviGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELR----AAG 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 488 GRVPAMALTAfAREEDRLR-AIEAGFQVHAIKPVQPAELAA 527
Cdd:cd19925    73 HDVDVIVVTA-ANDVETVReALRLGVVDYLIKPFTFERLRQ 112

glnL

PRK11073

nitrogen regulation protein NR(II);

168-383

9.75e-10

nitrogen regulation protein NR(II);

Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 60.48 E-value: 9.75e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 168 LSHELRTPLTAMLGWTQLLRSG----ALTADEEVrgleIIErnvlaQA----KLIDDLLdvsrivtGKLRLNVR-PLSLA 238
Cdd:PRK11073  137 LAHEIKNPLGGLRGAAQLLSKAlpdpALTEYTKV----IIE-----QAdrlrNLVDRLL-------GPQRPGTHvTESIH 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 239 SVIEAALDVV--RPAADAKAVR-FEPLLDEraghVTGDPDRLQQVVWNLLVNAVK-FSPVGGKIRV------SLTRQGSR 308
Cdd:PRK11073  201 KVAERVVQLVslELPDNVRLIRdYDPSLPE----LAHDPDQIEQVLLNIVRNALQaLGPEGGTITLrtrtafQLTLHGER 276

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 309 ----SQIEVADEGEGIDsdimPHIFDRFRQADSSTRrsHGGLGLGLAIVRHVVELHGGSVRAESLgAGHgATFVVELPL 383
Cdd:PRK11073  277 yrlaARIDIEDNGPGIP----PHLQDTLFYPMVSGR--EGGTGLGLSIARNLIDQHSGKIEFTSW-PGH-TEFSVYLPI 347

REC_hyHK_blue-like

cd18161

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...

416-520

9.96e-10

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381145 [Multi-domain] Cd Length: 102 Bit Score: 55.82 E-value: 9.96e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQ-ARPDVLISDIGMP-EEDGYDLIRRVRDLAPaeggRVPAM 493
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESgPDIDLLVTDVIMPgGMNGSQLAEEARRRRP----DLKVL 76

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAiKPV 520
Cdd:cd18161    77 LTSGYAENAIEGGDLAPGVDVLS-KPF 102

REC_DC-like

cd17534

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...

415-525

1.50e-09

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381089 [Multi-domain] Cd Length: 117 Bit Score: 55.88 E-value: 1.50e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVL-SVYHAQVATASSAREALALFAQARPDVLISDIGMPEE-DGYDLIRRVRDLAPaeggrVPA 492
Cdd:cd17534     2 KILIVEDEAIIALDLKEILeSLGYEVVGIADSGEEAIELAEENKPDLILMDINLKGDmDGIEAAREIREKFD-----IPV 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232315758 493 MALTAFAREEDRLRAIEA---GFqvhAIKPVQPAEL 525
Cdd:cd17534    77 IFLTAYSDEETLERAKETnpyGY---LVKPFNEREL 109

PRK11697

two-component system response regulator BtsR;

415-540

1.50e-09

two-component system response regulator BtsR;

Pssm-ID: 236956 [Multi-domain] Cd Length: 238 Bit Score: 58.70 E-value: 1.50e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYH--AQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRvrdLAPAEGGRVpa 492
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGdiEIVGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGM---LDPEHMPYI-- 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1232315758 493 MALTAFarEEDRLRAieagFQVHA----IKPVQPAELAAGVAKLAgRDASPS 540
Cdd:PRK11697   78 VFVTAF--DEYAIKA----FEEHAfdylLKPIDPARLAKTLARLR-QERSPQ 122

REC_OmpR_VirG

cd17594

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...

416-531

1.53e-09

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381125 [Multi-domain] Cd Length: 113 Bit Score: 55.53 E-value: 1.53e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRVPAMAL 495
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS-----DVPIIII 76

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1232315758 496 TAFAREE-DRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:cd17594    77 SGDRRDEiDRVVGLELGADDYLAKPFGLRELLARVRA 113

PRK10529

DNA-binding transcriptional activator KdpE; Provisional

416-543

1.55e-09

DNA-binding transcriptional activator KdpE; Provisional

Pssm-ID: 182522 [Multi-domain] Cd Length: 225 Bit Score: 58.28 E-value: 1.55e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggrVPAMAL 495
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSA-----IPVIVL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASPSGPN 543
Cdd:PRK10529   79 SARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATPAPD 126

PRK10643

two-component system response regulator PmrA;

415-535

2.62e-09

two-component system response regulator PmrA;

Pssm-ID: 182612 [Multi-domain] Cd Length: 222 Bit Score: 57.74 E-value: 2.62e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDlapaEGGRVPAMA 494
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ----KKYTLPVLI 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:PRK10643   78 LTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRR 118

REC_OmpR_BfmR-like

cd19939

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...

415-535

3.86e-09

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381166 [Multi-domain] Cd Length: 116 Bit Score: 54.69 E-value: 3.86e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEpdgrEAIAKVLSVY--HA--QVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRV 490
Cdd:cd19939     1 RILIVEDE----LELARLTRDYliKAglEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR-----EHSHV 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1232315758 491 PAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:cd19939    72 PILMLTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116

REC_OmpR_NsrR-like

cd18159

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...

416-511

7.06e-09

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381143 [Multi-domain] Cd Length: 113 Bit Score: 53.82 E-value: 7.06e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggrVPAMAL 495
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-----VPIIFI 75

                          90
                  ....*....|....*.
gi 1232315758 496 TAFAREEDRLRAIEAG 511
Cdd:cd18159    76 SSRDDNMDQVMAINMG 91

REC_DesR-like

cd19930

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...

416-531

7.45e-09

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381157 [Multi-domain] Cd Length: 117 Bit Score: 53.82 E-value: 7.45e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYH--AQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeGGRVpaM 493
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELP--DTKV--L 76

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:cd19930    77 IVTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114

PRK10610

chemotaxis protein CheY;

414-532

8.46e-09

chemotaxis protein CheY;

Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 54.21 E-value: 8.46e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVL-SVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGGRVPA 492
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLkELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIR--ADGAMSALPV 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232315758 493 MALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKL 532
Cdd:PRK10610   84 LMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKI 123

PRK11086

sensory histidine kinase DcuS; Provisional

264-382

9.38e-09

sensory histidine kinase DcuS; Provisional

Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 58.00 E-value: 9.38e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 264 DERAGHVtgdpdrLQQVVWNLLVN---AVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRfrqaDSSTR 340
Cdd:PRK11086  427 DEDQVHE------LITILGNLIENaleAVGGEE-GGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDK----GYSTK 495

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232315758 341 RShgGLGLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELP 382
Cdd:PRK11086  496 GS--NRGVGLYLVKQSVENLGGSIAVESE-PGVGTQFFVQIP 534

ompR

PRK09468

osmolarity response regulator; Provisional

415-527

1.09e-08

osmolarity response regulator; Provisional

Pssm-ID: 181883 [Multi-domain] Cd Length: 239 Bit Score: 56.14 E-value: 1.09e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMA 494
Cdd:PRK09468    7 KILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLR----SQNNPTPIIM 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:PRK09468   83 LTAKGEEVDRIVGLEIGADDYLPKPFNPRELLA 115

REC_typeA_ARR

cd17581

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...

416-525

1.11e-08

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381119 [Multi-domain] Cd Length: 122 Bit Score: 53.52 E-value: 1.11e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALF---------AQARPDV--LISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssNFNEPKVnmIITDYCMPGMTGYDLLKKVKESSA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232315758 485 AEggRVPAMALTAfAREEDRL-RAIEAGFQVHAIKPVQPAEL 525
Cdd:cd17581    81 LK--EIPVVIMSS-ENIPTRIsRCLEEGAEDFLLKPVKLADV 119

REC_Spo0A

cd17561

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...

414-519

1.17e-08

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381109 [Multi-domain] Cd Length: 108 Bit Score: 53.00 E-value: 1.17e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEpdgREaIAKVLSVYHAQ------VATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLapAEG 487
Cdd:cd17561     2 IKVLIADDN---RE-FVQLLEEYLNSqpdmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRM--RLE 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 488 GRVPAMALTAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd17561    76 KRPKIIMLTAFGQEDITQRAVELGASYYILKP 107

REC_RocR

cd17530

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...

415-533

1.18e-08

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381086 [Multi-domain] Cd Length: 123 Bit Score: 53.60 E-value: 1.18e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLS-VYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVrdlapAEGGRVPAM 493
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHL-----AESHSNAAV 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1232315758 494 ALT----AFAREEDRLRAIEAGFQVHAI--KPVQPAELAAGVAKLA 533
Cdd:cd17530    77 ILMsgldGGILESAETLAGANGLNLLGTlsKPFSPEELTELLTKYT 122

PRK10365

sigma-54-dependent response regulator transcription factor ZraR;

414-531

1.38e-08

sigma-54-dependent response regulator transcription factor ZraR;

Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 57.35 E-value: 1.38e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAM 493
Cdd:PRK10365    6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA----IPVL 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAK 531
Cdd:PRK10365   82 IMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119

REC_NarL

cd19931

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...

416-525

1.68e-08

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381158 [Multi-domain] Cd Length: 117 Bit Score: 52.74 E-value: 1.68e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSV--YHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAM 493
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIELdpDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALR----EEGVSARIV 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:cd19931    77 ILTVSDAEDDVVTALRAGADGYLLKDMEPEDL 108

PRK09836

DNA-binding transcriptional activator CusR; Provisional

414-539

2.04e-08

DNA-binding transcriptional activator CusR; Provisional

Pssm-ID: 182102 [Multi-domain] Cd Length: 227 Bit Score: 54.93 E-value: 2.04e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAM 493
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR----SANKGMPIL 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDASP 539
Cdd:PRK09836   77 LLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAV 122

REC_ETR-like

cd19933

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...

414-520

2.55e-08

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381160 [Multi-domain] Cd Length: 117 Bit Score: 52.40 E-value: 2.55e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPD--VLISDIGMPEEDGYDLIRRVRDLAPAEgGRVP 491
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLFGRR-ERPL 79

                          90       100
                  ....*....|....*....|....*....
gi 1232315758 492 AMALTAFAREEDRLRAIEAGFQVHAIKPV 520
Cdd:cd19933    80 IVALTANTDDSTREKCLSLGMNGVITKPV 108

REC_PilR

cd19926

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...

416-511

3.26e-08

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381153 [Multi-domain] Cd Length: 100 Bit Score: 51.38 E-value: 3.26e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMAL 495
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLP----QTPVAVI 76

                          90
                  ....*....|....*.
gi 1232315758 496 TAFAREEDRLRAIEAG 511
Cdd:cd19926    77 TAYGSLDTAIEALKAG 92

HATPase_CckA-like

cd16919

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...

277-382

4.02e-08

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: 51.61 E-value: 4.02e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQ---------------GSRSQIEVADEGEGIDSDIMPHIFDRFrqadSSTRR 341
Cdd:cd16919     1 LELAILNLAVNARDAMPEGGRLTIETSNQrvdadyalnyrdlipGNYVCLEVSDTGSGMPAEVLRRAFEPF----FTTKE 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 342 SHGGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16919    77 VGKGTGLGLSMVYGFVKQSGGHLRIYS-EPGVGTTVRIYLP 116

REC_TrxB

cd17595

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...

416-524

5.41e-08

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381126 [Multi-domain] Cd Length: 135 Bit Score: 51.95 E-value: 5.41e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVL-SVYHA--QVATASSAREALALFAQARPD-----VLISDIGMPEEDGYDLIRRVRDLAPaEG 487
Cdd:cd17595     3 ILTVDDDPQVLRAVARDLrRQYGKdyRVLRADSGAEALDALKELKLRgeavaLFLVDQRMPEMDGVEFLEKAMELFP-EA 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 488 GRVpamALTAFAREEDRLRAI-EAGFQVHAIKPVQPAE 524
Cdd:cd17595    82 KRV---LLTAYADTDAAIRAInDVQLDYYLLKPWDPPE 116

REC_RegA-like

cd17563

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...

415-484

9.31e-08

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381111 [Multi-domain] Cd Length: 112 Bit Score: 50.52 E-value: 9.31e-08

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQP 71

PRK15115

response regulator GlrR; Provisional

414-525

1.53e-07

response regulator GlrR; Provisional

Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 54.07 E-value: 1.53e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAM 493
Cdd:PRK15115    6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPG----MPVI 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:PRK15115   82 ILTAHGSIPDAVAATQQGVFSFLTKPVDRDAL 113

HATPase_Phy-like

cd16932

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...

272-365

1.82e-07

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.

Pssm-ID: 340409 [Multi-domain] Cd Length: 113 Bit Score: 49.58 E-value: 1.82e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 272 GDPDRLQQVVWNLLVNAVKFSPVGG---KIRVSLTRQGSRSQIEVAD-------EGEGIDSDIMPHIFDRFRQAdssTRR 341
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPSPGgwvEIKVSPTKKQIGDGVHVIHlefrithPGQGLPEELVQEMFEENQWT---TQE 78

                          90       100
                  ....*....|....*....|....
gi 1232315758 342 shgglGLGLAIVRHVVELHGGSVR 365
Cdd:cd16932    79 -----GLGLSISRKLVKLMNGDVR 97

REC_CheC-like

cd17593

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...

415-527

1.95e-07

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381124 [Multi-domain] Cd Length: 117 Bit Score: 49.84 E-value: 1.95e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSV-YHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDlapaEGGRVPAM 493
Cdd:cd17593     2 KVLICDDSSMARKQLARALPAdWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPV----EQLETKVI 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 494 ALTAFAREEDRLRAIEAGfqvhAI----KPVQPAELAA 527
Cdd:cd17593    78 VVSGDVQPEAKERVLELG----ALaflkKPFDPEKLAQ 111

pleD

PRK09581

response regulator PleD; Reviewed

410-527

2.91e-07

response regulator PleD; Reviewed

Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 52.98 E-value: 2.91e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 410 DLSGVRVLVVDDEPDGREAIAKVLSVYHAQVAtASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEGgr 489
Cdd:PRK09581  152 KDEDGRILLVDDDVSQAERIANILKEEFRVVV-VSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRY-- 228

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1232315758 490 VPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:PRK09581  229 VPILLLVDEDDDPRLVKALELGVNDYLMRPIDKNELLA 266

fixJ

PRK09390

response regulator FixJ; Provisional

416-496

3.16e-07

response regulator FixJ; Provisional

Pssm-ID: 181815 [Multi-domain] Cd Length: 202 Bit Score: 51.16 E-value: 3.16e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:PRK09390    6 VHVVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLK----ARGSPLPVIVM 81


                  .
gi 1232315758 496 T 496
Cdd:PRK09390   82 T 82

PRK10651

transcriptional regulator NarL; Provisional

414-533

4.42e-07

transcriptional regulator NarL; Provisional

Pssm-ID: 182619 [Multi-domain] Cd Length: 216 Bit Score: 50.80 E-value: 4.42e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQ--VATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAegGRVp 491
Cdd:PRK10651    7 ATILLIDDHPMLRTGVKQLISMAPDItvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLS--GRI- 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1232315758 492 aMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLA 533
Cdd:PRK10651   84 -VVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQAA 124

PRK11517

DNA-binding response regulator HprR;

414-529

1.12e-06

DNA-binding response regulator HprR;

Pssm-ID: 183172 [Multi-domain] Cd Length: 223 Bit Score: 49.90 E-value: 1.12e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAM 493
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR-----TAKQTPVI 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:PRK11517   76 CLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARV 111

REC_OmpR_RegX3-like

cd17621

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...

416-519

1.64e-06

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381136 [Multi-domain] Cd Length: 99 Bit Score: 46.81 E-value: 1.64e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRVPAMAL 495
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARS-----NVPVIMV 75

                          90       100
                  ....*....|....*....|....
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd17621    76 TAKDSEIDKVVGLELGADDYVTKP 99

psREC-like_D2_PleD

cd17539

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...

416-529

1.66e-06

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.

Pssm-ID: 381094 [Multi-domain] Cd Length: 124 Bit Score: 47.31 E-value: 1.66e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAqVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRVPAMAL 495
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEHE-VVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLE-----RTRQLPI 74

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1232315758 496 TAFAREEDR---LRAIEAGFQVHAIKPVQPAELAAGV 529
Cdd:cd17539    75 LAVADPGDRgrlIRALEIGVNDYLVRPIDPNELLARV 111

REC_Spo0F-like

cd17553

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...

415-534

2.20e-06

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381105 [Multi-domain] Cd Length: 117 Bit Score: 46.78 E-value: 2.20e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAeggrVPAMA 494
Cdd:cd17553     2 KILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDEN----IRVII 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAG 534
Cdd:cd17553    78 MTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117

REC_OmpR_ChvI-like

cd19936

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...

416-519

3.21e-06

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381163 [Multi-domain] Cd Length: 99 Bit Score: 45.90 E-value: 3.21e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMAL 495
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR-----QKSTLPVIFL 75

                          90       100
                  ....*....|....*....|....
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd19936    76 TSKDDEIDEVFGLRMGADDYITKP 99

REC_PhyR

cd17540

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...

415-531

3.31e-06

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381095 [Multi-domain] Cd Length: 117 Bit Score: 46.09 E-value: 3.31e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPdgreAIAK-----VLSVYHAQVATASSAREALALFAQARPDVLISDIGMpeEDGYDLIRRVRDLAPAEggR 489
Cdd:cd17540     2 RVLIIEDEP----LIAMdleqiVEDLGHQVVGIARTRDEAVALARRERPDLILADIQL--ADGSSGIDAVNEILTTH--D 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1232315758 490 VPAMALTAFAreeDRLRA---IEAGFQVhaIKPVQPAELAAGVAK 531
Cdd:cd17540    74 VPVIFVTAYP---ERLLTgerPEPTFLI--TKPFDPEMVKAAISQ 113

dpiB

PRK15053

sensor histidine kinase DpiB; Provisional

148-382

3.80e-06

sensor histidine kinase DpiB; Provisional

Pssm-ID: 185013 [Multi-domain] Cd Length: 545 Bit Score: 49.83 E-value: 3.80e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 148 NTLNSEAreaNRIKD--EFLATLSHElrtpltaMLGWTQLLrSGALTADEEVRGLEIIERNVLAQAKLIDDLLD------ 219
Cdd:PRK15053  326 STLNAQL---TQIKQyvESLRTLRHE-------HLNWMSTL-NGLLQMKEYDRVLEMVQGESQAQQQLIDSLREafadrq 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 220 VSRIVTGK--------LRLNVRPLSLASVIEAALDVVRPAAdakavrfepllderaghvtgdpdrlqqVVWNLLVNAVKF 291
Cdd:PRK15053  395 VAGLLFGKvqrarelgLKMVIVPGSQLSQLPPGLDSTEFAA---------------------------IVGNLLDNAFEA 447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 292 S---PVGGK-IRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRfrqaDSSTRRSHGG-LGLGLAIVRHVVELHGGSVRA 366
Cdd:PRK15053  448 SlrsDEGNKiVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQ----GVSTRADEPGeHGIGLYLIASYVTRCGGVITL 523

                         250
                  ....*....|....*.
gi 1232315758 367 ESlGAGHGATFVVELP 382
Cdd:PRK15053  524 ED-NDPCGTLFSIFIP 538

PLN03029

type-a response regulator protein; Provisional

412-525

4.86e-06

type-a response regulator protein; Provisional

Pssm-ID: 215544 [Multi-domain] Cd Length: 222 Bit Score: 47.72 E-value: 4.86e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 412 SGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFA-----QARPDV---------------LISDIGMPEED 471
Cdd:PLN03029    7 SQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddRSNPDTpsvspnshqevevnlIITDYCMPGMT 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1232315758 472 GYDLIRRVRDLAPAEGgrVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAEL 525
Cdd:PLN03029   87 GYDLLKKIKESSSLRN--IPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138

GAF

COG2203

GAF domain [Signal transduction mechanisms];

2-514

6.17e-06

GAF domain [Signal transduction mechanisms];

Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 49.04 E-value: 6.17e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758   2 SMEKMLQVITDTAREIIGAHRAtAVTTWDQNWARCKTTLSLSPEFGPRRPLLSPSSGCelhtlWLALGRAGRLSSAELLA 81
Cdd:COG2203   207 DLEELLQRILELAGELLGADRG-AILLVDEDGGELELVAAPGLPEEELGRLPLGEGLA-----GRALRTGEPVVVNDAST 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758  82 HPAWHTLGPSLCDFGQPPDWLAAPLTgRDGRDMGLLHVCGKCQGDFTSEDEAVLLQLAQMASIAIENTLNSEAREANRIK 161
Cdd:COG2203   281 DPRFAPSLRELLLALGIRSLLCVPLL-VDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 162 DEFLATLSHELRTPLTAMLGWTQLLRSGALTADEEVRGLEIIERNVLAQAKLIDDLLDVSRIVTGKLRLNVRPLSLASVI 241
Cdd:COG2203   360 LLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLL 439

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 242 EAALDVVRPAADAKAVRFEPLLDERAGHVTGDPDRLQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGID 321
Cdd:COG2203   440 RVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLL 519

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 322 SDIMPHIFDRFRQADSSTRRSHGGLGLGLAIVRHVVELHGGSVRAESLGAGHGATFVVELPLSAVVAEGHAQRPDTSAPR 401
Cdd:COG2203   520 LLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGD 599

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 402 AAAPRSEIDLSGVRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRD 481
Cdd:COG2203   600 LLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDSSLLLGLLLL 679

                         490       500       510
                  ....*....|....*....|....*....|...
gi 1232315758 482 LAPAEGGRVPAMALTAFAREEDRLRAIEAGFQV 514
Cdd:COG2203   680 GALLLLGGGLALLLSIGLGLGVARLLQLSVLEV 712

ComP

COG4585

Signal transduction histidine kinase ComP [Signal transduction mechanisms];

176-385

6.94e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];

Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 47.69 E-value: 6.94e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 176 LTAMLGWTQLLRSGALTADEEVRG-LEIIERnvlaqakLIDDLLDVSRIVTGKLR-LNVRPLSLASVIEAALDVVRPAAD 253
Cdd:COG4585    69 LSAIKLQLEAARRLLDADPEAAREeLEEIRE-------LAREALAELRRLVRGLRpPALDDLGLAAALEELAERLLRAAG 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 254 AKaVRFepllderagHVTGDPDRLQQVVWN--------LLVNAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIM 325
Cdd:COG4585   142 IR-VEL---------DVDGDPDRLPPEVELalyrivqeALTNALKHAG-ATRVTVTLEVDDGELTLTVRDDGVGFDPEAA 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 326 PhifdrfrqadsstrrshgGLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVELPLSA 385
Cdd:COG4585   211 P------------------GGGLGLRGMRERAEALGGTLTIGS-APGGGTRVRATLPLAA 251

PRK00742

chemotaxis-specific protein-glutamate methyltransferase CheB;

414-478

1.02e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;

Pssm-ID: 234828 [Multi-domain] Cd Length: 354 Bit Score: 47.84 E-value: 1.02e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLS------VyhaqVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRR 478
Cdd:PRK00742    4 IRVLVVDDSAFMRRLISEILNsdpdieV----VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEK 70

CheA

COG0643

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];

296-390

1.13e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];

Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 48.25 E-value: 1.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 296 GKIRVSLTRQGSRSQIEVADEGEGID------------------------SDIMPHIFdrfrQADSSTRR-----ShgGL 346
Cdd:COG0643   309 GTITLSAYHEGGRVVIEVSDDGRGLDlekirakaiekglitaeeaaalsdEELLELIF----APGFSTAEevtdlS--GR 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1232315758 347 GLGLAIVRHVVELHGGSVRAESLgAGHGATFVVELPLSAVVAEG 390
Cdd:COG0643   383 GVGMDVVKTNIEALGGTIEIESE-PGKGTTFTLRLPLTLAIIDG 425

HATPase_CheA-like

cd16916

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...

296-382

1.25e-05

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: 46.04 E-value: 1.25e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 296 GKIRVSLTRQGSRSQIEVADEGEGI------------------------DSDIMPHIFDR-FRQADSSTRRShgGLGLGL 350
Cdd:cd16916    70 GTITLRAEHQGNQVVIEVSDDGRGIdrekirekaierglitadeaatlsDDEVLNLIFAPgFSTAEQVTDVS--GRGVGM 147

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 351 AIVRHVVELHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16916   148 DVVKRSIESLGGTIEVES-EPGQGTTFTIRLP 178

PRK10693

two-component system response regulator RssB;

443-520

1.25e-05

two-component system response regulator RssB;

Pssm-ID: 182652 [Multi-domain] Cd Length: 303 Bit Score: 47.29 E-value: 1.25e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1232315758 443 ASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDlapaEGGRVPAMALTAFAREEDRLRAIEAGFQVHAIKPV 520
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRN----RGDQTPVLVISATENMADIAKALRLGVQDVLLKPV 76

REC_OmpR_CtrA

cd17616

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...

416-527

1.37e-05

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381132 [Multi-domain] Cd Length: 114 Bit Score: 44.32 E-value: 1.37e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMAL 495
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLR----LAKVKTPILIL 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17616    77 SGLADIEDKVKGLGFGADDYMTKPFHKDELVA 108

PRK15479

transcriptional regulator TctD;

415-537

1.56e-05

transcriptional regulator TctD;

Pssm-ID: 185376 [Multi-domain] Cd Length: 221 Bit Score: 46.25 E-value: 1.56e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapAEGGRVPAMA 494
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLR----KRGQTLPVLL 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGRDA 537
Cdd:PRK15479   78 LTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSA 120

PRK12555

chemotaxis-specific protein-glutamate methyltransferase CheB;

414-484

1.78e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;

Pssm-ID: 237135 [Multi-domain] Cd Length: 337 Bit Score: 47.18 E-value: 1.78e-05

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHA-QVA-TASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:PRK12555    1 MRIGIVNDSPLAVEALRRALARDPDhEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAERP 73

REC_RcNtrC-like

cd19928

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...

416-484

1.86e-05

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381155 [Multi-domain] Cd Length: 100 Bit Score: 43.65 E-value: 1.86e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKARP 69

PRK10710

DNA-binding transcriptional regulator BaeR; Provisional

415-535

1.99e-05

DNA-binding transcriptional regulator BaeR; Provisional

Pssm-ID: 182665 [Multi-domain] Cd Length: 240 Bit Score: 46.22 E-value: 1.99e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLApaeggRVPAMA 494
Cdd:PRK10710   12 RILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-----DIPIVM 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:PRK10710   87 VTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTILRR 127

glnG

PRK10923

nitrogen regulation protein NR(I); Provisional

416-497

2.55e-05

nitrogen regulation protein NR(I); Provisional

Pssm-ID: 182842 [Multi-domain] Cd Length: 469 Bit Score: 46.79 E-value: 2.55e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPaeggRVPAMAL 495
Cdd:PRK10923    6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHP----MLPVIIM 81


                  ..
gi 1232315758 496 TA 497
Cdd:PRK10923   82 TA 83

YesM

COG2972

Sensor histidine kinase YesM [Signal transduction mechanisms];

285-383

3.13e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];

Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 46.55 E-value: 3.13e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 285 LV-NAVK--FSPV--GGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADSSTrrshgglGLGLAIVRHVVEL 359
Cdd:COG2972   344 LVeNAIEhgIEPKegGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGEGR-------GIGLRNVRERLKL 416

                          90       100
                  ....*....|....*....|....*..
gi 1232315758 360 H---GGSVRAESlGAGHGATFVVELPL 383
Cdd:COG2972   417 YygeEYGLEIES-EPGEGTTVTIRIPL 442

REC_NtrC1-like

cd17572

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...

416-480

3.16e-05

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381114 [Multi-domain] Cd Length: 121 Bit Score: 43.34 E-value: 3.16e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 416 VLVVDDEPdgreAIAKVLSVY----HAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVR 480
Cdd:cd17572     1 VLLVEDSP----SLAALYQEYlsdeGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQ 65

HATPase_UhpB-NarQ-NarX-like

cd16917

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

279-382

3.26e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; 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 UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.

Pssm-ID: 340394 [Multi-domain] Cd Length: 87 Bit Score: 42.54 E-value: 3.26e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 279 QVVWNLLVNAVKFSPvGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPhifdrfrqadsstrrshGGLGLGLAIVRHVVE 358
Cdd:cd16917     3 RIVQEALTNALKHAG-ASRVRVTLSYTADELTLTVVDDGVGFDGPAPP-----------------GGGGFGLLGMRERAE 64

                          90       100
                  ....*....|....*....|....
gi 1232315758 359 LHGGSVRAESlGAGHGATFVVELP 382
Cdd:cd16917    65 LLGGTLTIGS-RPGGGTRVTARLP 87

COG3920

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...

231-388

3.45e-05

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

Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 46.44 E-value: 3.45e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 231 NVRPLSLASVIEAALDVVRPAADAKAVRFEPLLDEraghVTGDPDRLQQV--VWN-LLVNAVKF---SPVGGKIRVSLTR 304
Cdd:COG3920   355 DWEGVDLRDYLRELLEPLRDSYGGRGIRIELDGPD----VELPADAAVPLglILNeLVTNALKHaflSGEGGRIRVSWRR 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 305 QGSRSQIEVADEGEGIDSDImphifdrfrqaDSSTRRshgglGLGLAIVRHVVELHGGSVraeSLGAGHGATFVVELPLS 384
Cdd:COG3920   431 EDGRLRLTVSDNGVGLPEDV-----------DPPARK-----GLGLRLIRALVRQLGGTL---ELDRPEGTRVRITFPLA 491


                  ....
gi 1232315758 385 AVVA 388
Cdd:COG3920   492 ELAA 495

PRK10955

envelope stress response regulator transcription factor CpxR;

415-527

3.81e-05

envelope stress response regulator transcription factor CpxR;

Pssm-ID: 182864 [Multi-domain] Cd Length: 232 Bit Score: 45.18 E-value: 3.81e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFaQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMA 494
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLL-DDSIDLLLLDVMMPKKNGIDTLKELR-----QTHQTPVIM 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:PRK10955   77 LTARGSELDRVLGLELGADDYLPKPFNDRELVA 109

REC_FixJ

cd17537

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...

416-482

4.34e-05

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381092 [Multi-domain] Cd Length: 116 Bit Score: 42.97 E-value: 4.34e-05

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDL 482
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLAR 69

HATPase_NtrY-like

cd16944

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

273-382

5.37e-05

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: 42.52 E-value: 5.37e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 273 DPDRLQQVVWNLLVNA------VKFSPVGGKIRVSlTRQGSRSQIEVADEGEGIDsdimPHIFDRFRQADSSTRRShgGL 346
Cdd:cd16944     1 DTTQISQVLTNILKNAaeaiegRPSDVGEVRIRVE-ADQDGRIVLIVCDNGKGFP----REMRHRATEPYVTTRPK--GT 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1232315758 347 GLGLAIVRHVVELHGGSVRAESLGAGhGATFVVELP 382
Cdd:cd16944    74 GLGLAIVKKIMEEHGGRISLSNREAG-GACIRIILP 108

REC_WspR-like

cd17575

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...

414-527

8.01e-05

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381117 [Multi-domain] Cd Length: 128 Bit Score: 42.39 E-value: 8.01e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLS-----VYHaqvaTASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlAPAEGG 488
Cdd:cd17575     1 IMVLLVDDQAIIGEAVRRALAdeediDFH----YCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFR--ANPATR 74

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1232315758 489 RVPAMALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:cd17575    75 DIPIIVLSTKEEPEVKSEAFALGANDYLVKLPDKIELVA 113

PRK15369

two component system response regulator;

414-511

9.21e-05

two component system response regulator;

Pssm-ID: 185267 [Multi-domain] Cd Length: 211 Bit Score: 43.91 E-value: 9.21e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVY-HAQVAtaSSAREALALFAQAR---PDVLISDIGMPEEDGYDLIRRVRDlapaeggR 489
Cdd:PRK15369    4 YKILLVDDHELIINGIKNMLAPYpRYKIV--GQVDNGLEVYNACRqlePDIVILDLGLPGMNGLDVIPQLHQ-------R 74

                          90       100
                  ....*....|....*....|....*
gi 1232315758 490 VPAM---ALTAFAREEDRLRAIEAG 511
Cdd:PRK15369   75 WPAMnilVLTARQEEHMASRTLAAG 99

HATPase_YpdA-YehU-LytS-like

cd16924

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

277-361

1.13e-04

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

Pssm-ID: 340401 [Multi-domain] Cd Length: 103 Bit Score: 41.66 E-value: 1.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 277 LQQVVWNLLVNAVKFSPVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPhifdrfrqadSSTRRSHGGLGLGLAIVRH- 355
Cdd:cd16924     6 LQPLVENAIQHGLSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLN----------ILGKKPKEGNGIGLYNVHQr 75


                  ....*.
gi 1232315758 356 VVELHG 361
Cdd:cd16924    76 LILLFG 81

GAF

pfam01590

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...

2-146

1.13e-04

Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 42.08 E-value: 1.13e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758   2 SMEKMLQVITDTAREIIGAHRATAvttWDQNWARCKTTLSLSPEFGPRRPLLSPSSGCELhtlwLALGRAgrLSSAELLA 81
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCAL---YLPDADGLEYLPPGARWLKAAGLEIPPGTGVTV----LRTGRP--LVVPDAAG 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758  82 HPAWHTLGPSLCDFGqPPDWLAAPLTgRDGRDMGLLhVCGKCQGDFTSEDEAVLLQLAQMASIAI 146
Cdd:pfam01590  72 DPRFLDPLLLLRNFG-IRSLLAVPII-DDGELLGVL-VLHHPRPPFTEEELELLEVLADQVAIAL 133

PRK10701

DNA-binding transcriptional regulator RstA; Provisional

415-527

1.22e-04

DNA-binding transcriptional regulator RstA; Provisional

Pssm-ID: 236738 [Multi-domain] Cd Length: 240 Bit Score: 43.86 E-value: 1.22e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLirrVRDLAPAEGGrvPAMA 494
Cdd:PRK10701    3 KIVFVEDDAEVGSLIAAYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTI---CRDLRPKWQG--PIVL 77

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAA 527
Cdd:PRK10701   78 LTSLDSDMNHILALEMGACDYILKTTPPAVLLA 110

REC_PatA-like

cd17602

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...

416-519

1.70e-04

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.

Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 40.81 E-value: 1.70e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 416 VLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAPAEggRVPAMAL 495
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALK--DTPIIML 78

                          90       100
                  ....*....|....*....|....
gi 1232315758 496 TAFAREEDRLRAIEAGFQVHAIKP 519
Cdd:cd17602    79 TGKDGLVDRIRAKMAGASGYLTKP 102

PRK10815

two-component system sensor histidine kinase PhoQ;

272-368

2.58e-04

two-component system sensor histidine kinase PhoQ;

Pssm-ID: 182754 [Multi-domain] Cd Length: 485 Bit Score: 43.85 E-value: 2.58e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 272 GDPDRLQQVVWNLLVNAVK----FspvggkIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDRFRQADssTRRShgGLG 347
Cdd:PRK10815  374 GEKNDFMEVMGNVLDNACKycleF------VEISARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRAD--TLRP--GQG 443

                          90       100
                  ....*....|....*....|.
gi 1232315758 348 LGLAIVRHVVELHGGSVRAES 368
Cdd:PRK10815  444 LGLSVAREITEQYEGKISAGD 464

PRK10618

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional

131-339

2.60e-04

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional

Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 44.15 E-value: 2.60e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 131 DEAVL----LQLAQMasiaiENTLNSEAREAnrikdeFLATLSHELRTPLTAMlgwTQLLRSGALTADEEVRGLEIieRN 206
Cdd:PRK10618  427 DREVLvnkkLQQAQR-----EYEKNQQARKA------FLQNIGDELKQPLQSL---AQLAAQLRQTSDEEQQQPEL--DQ 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 207 VLAQA----KLIDDLLDVSRIVTGKLRLNVRPLSLASVIEAALDVVRPAADAKA----VRFEPLLDEragHVTGDPDRLQ 278
Cdd:PRK10618  491 LAEQSdvlvRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGlqllIHNHLKAEQ---LRIGDRDALR 567

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315758 279 QVVWNLLVNAVKFSPVgGKIRVSLTRQGSRS---QIEVADEGEGIDSDIM---------PHIFDRFRQADSST 339
Cdd:PRK10618  568 KILLLLLNYAITTTAY-GKITLEVDQDESSPdrlTIRILDTGAGVSIKELdnlhfpflnQTQGDRYGKASGLT 639

RsbW

COG2172

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

275-381

3.28e-04

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

Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 40.67 E-value: 3.28e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 275 DRLQQVVWNLLVNAVKFS---PVGGKIRVSLTRQGSRSQIEVADEGEGIDSDIMPHIFDrfrqadsstrrSHGGLGLGLA 351
Cdd:COG2172    33 DDLVLAVSEAVTNAVRHAyggDPDGPVEVELELDPDGLEIEVRDEGPGFDPEDLPDPYS-----------TLAEGGRGLF 101

                          90       100       110
                  ....*....|....*....|....*....|
gi 1232315758 352 IVRHVVElhggSVRAESLGAGHGATFVVEL 381
Cdd:COG2172   102 LIRRLMD----EVEYESDPGGTTVRLVKRL 127

PRK10336

two-component system response regulator QseB;

414-553

5.54e-04

two-component system response regulator QseB;

Pssm-ID: 182387 [Multi-domain] Cd Length: 219 Bit Score: 41.42 E-value: 5.54e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 414 VRVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDlapaEGGRVPAM 493
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWRE----KGQREPVL 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1232315758 494 ALTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAgRDASPSGPNGDGHG-VSANP 553
Cdd:PRK10336   77 ILTARDALAERVEGLRLGADDYLCKPFALIEVAARLEALM-RRTNGQASNELRHGnVMLDP 136

GAF_2

pfam13185

GAF domain; The GAF domain is named after some of the proteins it is found in, including ...

1-147

1.02e-03

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).

Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 39.37 E-value: 1.02e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758   1 MSMEKMLQVITDTAREIiGAHRATAVttWDQNWARCKTTLSLSPEFGPRRPLLSPSSGcelhTLWLALGRAGRLSSAELL 80
Cdd:pfam13185   2 ADLEELLDAVLEAAVEL-GASAVGFI--LLVDDDGRLAAWGGAADELSAALDDPPGEG----LVGEALRTGRPVIVNDLA 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1232315758  81 AHPAWHTLGPSLCDFGqppDWLAAPLTgRDGRDMGLLHVCGKCQGDFTSEDEAVLLQLAQMASIAIE 147
Cdd:pfam13185  75 ADPAKKGLPAGHAGLR---SFLSVPLV-SGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137

GAF

smart00065

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...

7-150

2.77e-03

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.

Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 38.52 E-value: 2.77e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758    7 LQVITDTAREIIGAHRATAVTTWDQNWARCKTTLSlspeFGPRRPLLSPSSGCELHTLWLALGRAGRLSSAELLAHPAWH 86
Cdd:smart00065   6 LQTILEELRQLLGADRVLIYLVDENDRGELVLVAA----DGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLFA 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1232315758   87 tlGPSLCDFGQPPDWLAAPLTgRDGRDMGLLHVCGKCQGD-FTSEDEAVLLQLAQMASIAIENTL 150
Cdd:smart00065  82 --EDLLGRYQGVRSFLAVPLV-ADGELVGVLALHNKKSPRpFTEEDEELLQALANQLAIALANAQ 143

PRK10766

two-component system response regulator TorR;

415-535

3.31e-03

two-component system response regulator TorR;

Pssm-ID: 182711 [Multi-domain] Cd Length: 221 Bit Score: 39.25 E-value: 3.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 415 RVLVVDDEPDGREAIAKVLSVYHAQVATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRdlapaEGGRVPAMA 494
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR-----SRSTVGIIL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1232315758 495 LTAFAREEDRLRAIEAGFQVHAIKPVQPAELAAGVAKLAGR 535
Cdd:PRK10766   79 VTGRTDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLLWR 119

REC_GlnL-like

cd17565

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...

418-484

4.83e-03

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381112 [Multi-domain] Cd Length: 103 Bit Score: 36.87 E-value: 4.83e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1232315758 418 VVDDEPdgreAIAKVLSVYHAQ------VATASSAREALALFAQARPDVLISDIGMPEEDGYDLIRRVRDLAP 484
Cdd:cd17565     3 IVDDDK----NIIKILSDIIEDddlgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGS 71

HATPase_RsbW-like

cd16936

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...

284-372

4.98e-03

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.

Pssm-ID: 340413 [Multi-domain] Cd Length: 91 Bit Score: 36.48 E-value: 4.98e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 284 LLVNAVKF---SPVGGKIRVSLTRQGSRSQIEVADEGEGidsdimphiFDRFRQADSSTRRSHGglGLGLAIVRHVVElh 360
Cdd:cd16936     8 AVTNAVRHayrHDGPGPVRLELDLDPDRLRVEVTDSGPG---------FDPLRPADPDAGLREG--GRGLALIRALMD-- 74

                          90
                  ....*....|..
gi 1232315758 361 ggSVRAESLGAG 372
Cdd:cd16936    75 --EVGYRRTPGG 84

HATPase_ETR2_ERS2-EIN4-like

cd16938

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...

270-381

5.99e-03

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.

Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 37.44 E-value: 5.99e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1232315758 270 VTGDPDRLQQVVWNLLVNAVKFSPVGGKI--RVSLTRQGS---------------------RSQIEVADEGEG-IDSDIM 325
Cdd:cd16938     5 VVGDERRVFQVLLHMLGNLLKMRNGGGNItfRVFLEGGSEdrsdrdwgpwrpsmsdesveiRFEVEINDSGSPsIESASM 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1232315758 326 PHifdrfrqadSSTRRSHG---GLGLGLAIVRHVVELHGGSVRAESlGAGHGATFVVEL 381
Cdd:cd16938    85 RN---------SLNRRYNLselGEHLSFSICKQLVQLMGGNIWIVP-GSGLGTTMSLLL 133

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