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Conserved domains on  [gi|2575951464|ref|WP_309421992|]
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ATP-binding protein [Eggerthella sp.]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
425-682 2.67e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.45  E-value: 2.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 425 LLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDdrEKVAETLKKIGDASDH 504
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD--EEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 505 LLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVfVGDARRIKQLLLNLLTNA 584
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 585 VKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPF-SMEGRSREQGTGLGMPIVKNIVTMMAGDI 663
Cdd:COG0642   236 IKYTPEGGTVTVSVRREGD------RVRISVEDTGPGIPPEDLERIFEPFfRTDPSRRGGGTGLGLAIVKRIVELHGGTI 309
                         250
                  ....*....|....*....
gi 2575951464 664 AVESTKGQGTTFTVTFNLR 682
Cdd:COG0642   310 EVESEPGKGTTFTVTLPLA 328
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
747-877 2.79e-38

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: 138.83  E-value: 2.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 747 TEFEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldRE 826
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIRA--LP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 827 DADAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
307-469 4.94e-03

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 307 RRRLREQNVAMLGQLYEALSDSIDMAvnlysPTDGKVTPIVAKAERIIGYRLDAFL-QNERLAATIGLSPEGVALFDRIR 385
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIIT-----DLDGRILYVNPAFERLTGYSAEELLgKTLRDLLPPEDDDEFLELLRAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 386 KDEtkGFEQGEFSFRSKQtGKECWASYSVKRLTFED--KPQLLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRM 463
Cdd:COG2202    77 AGG--GVWRGELRNRRKD-GSLFWVELSISPVRDEDgeITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153

                  ....*.
gi 2575951464 464 SHEIRT 469
Cdd:COG2202   154 DLDGRI 159
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
425-682 2.67e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.45  E-value: 2.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 425 LLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDdrEKVAETLKKIGDASDH 504
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD--EEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 505 LLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVfVGDARRIKQLLLNLLTNA 584
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 585 VKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPF-SMEGRSREQGTGLGMPIVKNIVTMMAGDI 663
Cdd:COG0642   236 IKYTPEGGTVTVSVRREGD------RVRISVEDTGPGIPPEDLERIFEPFfRTDPSRRGGGTGLGLAIVKRIVELHGGTI 309
                         250
                  ....*....|....*....
gi 2575951464 664 AVESTKGQGTTFTVTFNLR 682
Cdd:COG0642   310 EVESEPGKGTTFTVTLPLA 328
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
445-873 2.09e-67

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: 242.76  E-value: 2.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 445 AMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKvAETLKKIGDASDHLLGLINDVLDISKIENGKMT 524
Cdd:TIGR02956 453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQ-QQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 525 LASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVGDARRIKQLLLNLLTNAVKYTPcGGCVRFETTVAKGa 604
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRVSLNDD- 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 605 amgyRQVKFTVSDNGIGMSEEFKEHIFEPFS-MEGRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTfnlri 683
Cdd:TIGR02956 610 ----SSLLFEVEDTGCGIAEEEQATLFDAFTqADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFT----- 680
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 684 aleaerIVFEEGEGAE-ADDAQPLELdaasaaalrslgardrlasrpvsayeapmpgapraldrtefEGLRVLLAEDNDL 762
Cdd:TIGR02956 681 ------LPLTRGKPAEdSATLTVIDL-----------------------------------------PPQRVLLVEDNEV 713
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 763 NAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDREDaDAVPIIAMSANAFA 842
Cdd:TIGR02956 714 NQMVAQGFLTRLGHKVTLAESGQSALECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFN 789
                         410       420       430
                  ....*....|....*....|....*....|.
gi 2575951464 843 EDVSASLASGMNAHLSKPIDMRRVLATLIKY 873
Cdd:TIGR02956 790 EDVAQYLAAGFDGFLAKPVVEEQLTAMIAVI 820
PRK15347 PRK15347
two component system sensor kinase;
445-874 2.50e-64

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 233.38  E-value: 2.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 445 AMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDRE--KVAETLKKigdASDHLLGLINDVLDISKIENGK 522
Cdd:PRK15347  387 AKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEqmDLADTARQ---CTLSLLAIINNLLDFSRIESGQ 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 523 MTLASEPFRLSAVLSHVASAVRVqceqRAQE-------FVVTTPPcadAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVr 595
Cdd:PRK15347  464 MTLSLEETALLPLLDQAMLTIQG----PAQSksltlrtFVGAHVP---LYLHLDSLRLRQILVNLLGNAVKFTETGGIR- 535
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 596 feTTVAKGAAMGYrqvkFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTF 675
Cdd:PRK15347  536 --LRVKRHEQQLC----FTVEDTGCGIDIQQQQQIFTPF-YQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCF 608
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 676 TvtfnLRIALEAerivFEEGEGAEADDAQPLELdaasAAALRSLGARDrLASRPVSAYEAP----MPGAPRALDRTEFEG 751
Cdd:PRK15347  609 S----LVLPLNE----YAPPEPLKGELSAPLAL----HRQLSAWGITC-QPGHQNPALLDPelayLPGRLYDLLQQIIQG 675
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 ---------------LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEA 816
Cdd:PRK15347  676 apnepvinlplqpwqLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEA---LELGRQHRFDLVLMDIRMPGLDGLET 752
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 817 TRCIRE----LDREdadaVPIIAMSANAFAEDVSASLASGMNAHLSKPIdmrrVLATLIKYV 874
Cdd:PRK15347  753 TQLWRDdpnnLDPD----CMIVALTANAAPEEIHRCKKAGMNHYLTKPV----TLAQLARAL 806
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
747-877 2.79e-38

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: 138.83  E-value: 2.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 747 TEFEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldRE 826
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIRA--LP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 827 DADAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
754-870 3.28e-37

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: 135.29  E-value: 3.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREDADaVPI 833
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEA---LELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRR-TPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17546    77 IALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
568-682 6.27e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 6.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  568 GDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSM--EGRSREQGT 645
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD------HVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2575951464  646 GLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLR 682
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
573-679 1.66e-33

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: 124.25  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE-QGTGLGMPI 651
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGD------GVVLEVEDNGPGIPEEDLERIFERFYRGDKSREgGGTGLGLAI 74
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 652 VKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd00075    75 VRRIVEAHGGRITVESEPGGGTTFTVTL 102
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
568-683 7.17e-32

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: 119.78  E-value: 7.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 568 GDARRIKQLLLNLLTNAVKYTPCGGCVRFetTVAKGAamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGTGL 647
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITV--TLSEGG-----ELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 648 GMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLRI 683
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
754-870 1.39e-22

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: 93.37  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDredaDAVPI 833
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---PDLILLDINMPGMDGLELLKRIRRRD----PTTPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
456-679 2.63e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.89  E-value: 2.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 456 KSEFLSRMSHEIRTPMNVILGTLQLARS--NPDDREKVAETLKKIGDasdhLLGLINDVLDISKIENGKMTLASEPFRLS 533
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAIQDgiRKFTPESLDSLQAEVGT----LTKLVDDLHDLSMSDEGALAYQKASVDLV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 534 AVLSHVASAVRVQCEQRAQEFVVTTPpcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFEttvakgAAMGYRQVKF 613
Cdd:NF012163  316 PLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHIS------ASQRPKEVTL 387
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:NF012163  388 TVADSAPGVSDEQLARLFERFYRVEVSRNRasgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTL 456
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
459-678 5.74e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 94.32  E-value: 5.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPmnviLGTLQLARSN-PDDREKV-------AETLKKIGDASDHLLgliNDVLDISKIENGKMTLASEPF 530
Cdd:NF040691  274 FVSDVSHELRTP----LTTIRMAADViHDSRDDFdpatarsAELLHTELDRFESLL---SDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 531 RLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVgDARRIKQLLLNLLTNAVKYtpcGGCVRFETTVakgaAMGYRQ 610
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEV-DPRRVERVLRNLVVNAIEH---GEGKPVVVTV----AQDDTA 418
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 611 VKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:NF040691  419 VAVTVRDHGVGLKPGEVALVFDRFWRADPARARttgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
753-863 2.11e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 67.18  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRedadAVP 832
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP---DVVLMDIRMPEMDGIKALKEMRSHET----RTP 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDM 863
Cdd:PRK11361   79 VILMTAYAEVETAVEALRCGAFDYVIKPFDL 109
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
752-809 1.44e-09

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: 54.50  E-value: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2575951464  752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMP 809
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK---PDLILLDIMMP 55
PAS COG2202
PAS domain [Signal transduction mechanisms];
307-469 4.94e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 307 RRRLREQNVAMLGQLYEALSDSIDMAvnlysPTDGKVTPIVAKAERIIGYRLDAFL-QNERLAATIGLSPEGVALFDRIR 385
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIIT-----DLDGRILYVNPAFERLTGYSAEELLgKTLRDLLPPEDDDEFLELLRAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 386 KDEtkGFEQGEFSFRSKQtGKECWASYSVKRLTFED--KPQLLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRM 463
Cdd:COG2202    77 AGG--GVWRGELRNRRKD-GSLFWVELSISPVRDEDgeITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153

                  ....*.
gi 2575951464 464 SHEIRT 469
Cdd:COG2202   154 DLDGRI 159
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
425-682 2.67e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 254.45  E-value: 2.67e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 425 LLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDdrEKVAETLKKIGDASDH 504
Cdd:COG0642    79 LLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELD--EEQREYLETILRSADR 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 505 LLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVfVGDARRIKQLLLNLLTNA 584
Cdd:COG0642   157 LLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTV-RGDPDRLRQVLLNLLSNA 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 585 VKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPF-SMEGRSREQGTGLGMPIVKNIVTMMAGDI 663
Cdd:COG0642   236 IKYTPEGGTVTVSVRREGD------RVRISVEDTGPGIPPEDLERIFEPFfRTDPSRRGGGTGLGLAIVKRIVELHGGTI 309
                         250
                  ....*....|....*....
gi 2575951464 664 AVESTKGQGTTFTVTFNLR 682
Cdd:COG0642   310 EVESEPGKGTTFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
442-679 1.41e-75

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 246.36  E-value: 1.41e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 442 MKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPD-DREKVAETLKKIGDASDHLLGLINDVLDISKIEN 520
Cdd:COG2205     2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDlSPEERRELLEIIRESAERLLRLIEDLLDLSRLES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 521 GKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTV 600
Cdd:COG2205    82 GKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPP-ELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 601 AKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPF-SMEGRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG2205   161 EGD------GVRISVSDNGPGIPEEELERIFERFyRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
277-682 1.15e-72

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 244.08  E-value: 1.15e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 277 AAVVTTTFEAVFAIIFACLVVVALLVFGAYRRRLREQNVAMLGQLYEALSDSIDMAVNLYSPTDGKVTPIVAKAERIIGY 356
Cdd:COG5002     3 LLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 357 RLDAFLQNERLAATIGLSPEGVALFDRIRKDETKGFEQGEFSFRSKQTGkecWASYSVKRLTFEDKPQLLVVMRDVTAdk 436
Cdd:COG5002    83 LLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLL---GRLSLRLSALLLGLLLLAAVERDITE-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 437 eiqlsmkdamdvAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNP-DDREKVAETLKKIGDASDHLLGLINDVLDI 515
Cdd:COG5002   158 ------------LERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAaDDPEERREYLEIILEEAERLSRLVNDLLDL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 516 SKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVR 595
Cdd:COG5002   226 SRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPE-DPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTIT 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 596 FETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSM--EGRSREQ-GTGLGMPIVKNIVTMMAGDIAVESTKGQG 672
Cdd:COG5002   305 VSLREEDD------QVRISVRDTGIGIPEEDLPRIFERFYRvdKSRSRETgGTGLGLAIVKHIVEAHGGRIWVESEPGKG 378
                         410
                  ....*....|
gi 2575951464 673 TTFTVTFNLR 682
Cdd:COG5002   379 TTFTITLPLA 388
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
445-873 2.09e-67

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: 242.76  E-value: 2.09e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 445 AMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKvAETLKKIGDASDHLLGLINDVLDISKIENGKMT 524
Cdd:TIGR02956 453 ARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQ-QQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 525 LASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVGDARRIKQLLLNLLTNAVKYTPcGGCVRFETTVAKGa 604
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRVSLNDD- 609
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 605 amgyRQVKFTVSDNGIGMSEEFKEHIFEPFS-MEGRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTfnlri 683
Cdd:TIGR02956 610 ----SSLLFEVEDTGCGIAEEEQATLFDAFTqADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFT----- 680
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 684 aleaerIVFEEGEGAE-ADDAQPLELdaasaaalrslgardrlasrpvsayeapmpgapraldrtefEGLRVLLAEDNDL 762
Cdd:TIGR02956 681 ------LPLTRGKPAEdSATLTVIDL-----------------------------------------PPQRVLLVEDNEV 713
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 763 NAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDREDaDAVPIIAMSANAFA 842
Cdd:TIGR02956 714 NQMVAQGFLTRLGHKVTLAESGQSALECFHQHA---FDLALLDINLPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFN 789
                         410       420       430
                  ....*....|....*....|....*....|.
gi 2575951464 843 EDVSASLASGMNAHLSKPIDMRRVLATLIKY 873
Cdd:TIGR02956 790 EDVAQYLAAGFDGFLAKPVVEEQLTAMIAVI 820
PRK15347 PRK15347
two component system sensor kinase;
445-874 2.50e-64

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 233.38  E-value: 2.50e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 445 AMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDRE--KVAETLKKigdASDHLLGLINDVLDISKIENGK 522
Cdd:PRK15347  387 AKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEqmDLADTARQ---CTLSLLAIINNLLDFSRIESGQ 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 523 MTLASEPFRLSAVLSHVASAVRVqceqRAQE-------FVVTTPPcadAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVr 595
Cdd:PRK15347  464 MTLSLEETALLPLLDQAMLTIQG----PAQSksltlrtFVGAHVP---LYLHLDSLRLRQILVNLLGNAVKFTETGGIR- 535
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 596 feTTVAKGAAMGYrqvkFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTF 675
Cdd:PRK15347  536 --LRVKRHEQQLC----FTVEDTGCGIDIQQQQQIFTPF-YQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCF 608
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 676 TvtfnLRIALEAerivFEEGEGAEADDAQPLELdaasAAALRSLGARDrLASRPVSAYEAP----MPGAPRALDRTEFEG 751
Cdd:PRK15347  609 S----LVLPLNE----YAPPEPLKGELSAPLAL----HRQLSAWGITC-QPGHQNPALLDPelayLPGRLYDLLQQIIQG 675
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 ---------------LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEA 816
Cdd:PRK15347  676 apnepvinlplqpwqLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEA---LELGRQHRFDLVLMDIRMPGLDGLET 752
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 817 TRCIRE----LDREdadaVPIIAMSANAFAEDVSASLASGMNAHLSKPIdmrrVLATLIKYV 874
Cdd:PRK15347  753 TQLWRDdpnnLDPD----CMIVALTANAAPEEIHRCKKAGMNHYLTKPV----TLAQLARAL 806
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
309-679 3.05e-55

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 195.07  E-value: 3.05e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 309 RLREQNvAMLGQLYEALSDSIdMAVNLysptDGKVTPIVAKAERIIGYRLDAfLQNERLAATIGLSPEGVALFDRIRKdE 388
Cdd:COG3852     1 ALRESE-ELLRAILDSLPDAV-IVLDA----DGRITYVNPAAERLLGLSAEE-LLGRPLAELFPEDSPLRELLERALA-E 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 389 TKGFEQGEFSFRSKQtGKECWASYSVKRLTFED-KPQLLVVMRDVTADKEIQlsmkDAMDVAEAANAAKsEFLSRMSHEI 467
Cdd:COG3852    73 GQPVTEREVTLRRKD-GEERPVDVSVSPLRDAEgEGGVLLVLRDITERKRLE----RELRRAEKLAAVG-ELAAGLAHEI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 468 RTPMNVILGTLQLARSNPDDrEKVAETLKKIGDASDHLLGLINDVLDISKIENGKMtlasEPFRLSAVLSHVASAVRVQC 547
Cdd:COG3852   147 RNPLTGIRGAAQLLERELPD-DELREYTQLIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLERVLELLRAEA 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 548 EQRAQeFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAMGYRQ----VKFTVSDNGIGMS 623
Cdd:COG3852   222 PKNIR-IVRDYDPSLPEVL-GDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQVTLGGLRprlyVRIEVIDNGPGIP 299
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 624 EEFKEHIFEPF-SmegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG3852   300 EEILDRIFEPFfT----TKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYL 352
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
430-873 6.32e-53

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 198.24  E-value: 6.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 430 RDVTADKEIQlsmkdamDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAEtLKKIgDASDHLLGLI 509
Cdd:PRK11091  264 RDITERKRYQ-------DALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKY-LKTI-HVSAITLGNI 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 510 -NDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVV-TTPPCADAVFVgDARRIKQLLLNLLTNAVKY 587
Cdd:PRK11091  335 fNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLePLLPLPHKVIT-DGTRLRQILWNLISNAVKF 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 588 TPCGGcVRFETTVAKGAamgyrQVKFTVSDNGIGMSEEFKEHIFEPF----SMEGRSREQGTGLGMPIVKNIVTMMAGDI 663
Cdd:PRK11091  414 TQQGG-VTVRVRYEEGD-----MLTFEVEDSGIGIPEDELDKIFAMYyqvkDSHGGKPATGTGIGLAVSKRLAQAMGGDI 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 664 AVESTKGQGTTFTVTFNLrialeaeRIVFEEGEGAEADDAQPLeldaasaaalrslgardrlasrpvsayeapmpgapra 743
Cdd:PRK11091  488 TVTSEEGKGSCFTLTIHA-------PAVAEEVEDAFDEDDMPL------------------------------------- 523
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 744 ldrtefEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREL 823
Cdd:PRK11091  524 ------PALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDE---YDLVLLDIQLPDMTGLDIARELRER 594
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2575951464 824 DREDaDAVPIIAMSANAFAeDVSASLASGMNAHLSKPIDMRRVLATLIKY 873
Cdd:PRK11091  595 YPRE-DLPPLVALTANVLK-DKKEYLDAGMDDVLSKPLSVPALTAMIKKF 642
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
428-878 1.17e-51

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 195.58  E-value: 1.17e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 428 VMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQL--ARSNPDDrekVAETLKKIGDASDHL 505
Cdd:PRK10841  419 VLVDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLlqTKELPKG---VDRLVTAMNNSSSLL 495
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 506 LGLINDVLDISKIENGKMTLASEPFRLSAVLSHVAS-----AVRVQ----CeqraqeFVvtTPPCADAVFvGDARRIKQL 576
Cdd:PRK10841  496 LKIISDILDFSKIESEQLKIEPREFSPREVINHITAnylplVVKKRlglyC------FI--EPDVPVALN-GDPMRLQQV 566
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 577 LLNLLTNAVKYTPCGgCVRFETTVAKGaamgYrqVKFTVSDNGIGMSEEFKEHIFEPF--SMEGRSRE-QGTGLGMPIVK 653
Cdd:PRK10841  567 ISNLLSNAIKFTDTG-CIVLHVRVDGD----Y--LSFRVRDTGVGIPAKEVVRLFDPFfqVGTGVQRNfQGTGLGLAICE 639
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 654 NIVTMMAGDIAVESTKGQGTTFTVTF--------------------------NLRIA--LEAE------RIVFEEGEGAE 699
Cdd:PRK10841  640 KLINMMDGDISVDSEPGMGSQFTIRIplygaqypqkkgveglqgkrcwlavrNASLEqfLETLlqrsgiQVQRYEGQEPT 719
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 700 ADDA----QPLELDAASAAALRSLGARDRLASRPVSAY---------------------EAPMPGAPRAL-----DRTEF 749
Cdd:PRK10841  720 PEDVlitdDPVQKKWQGRAVITFCRRHIGIPLEIAPGEwvhstatphelpallariyriELESDDSANALpstdkAVSDN 799
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDRedad 829
Cdd:PRK10841  800 DDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDA---LNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGL---- 872
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 830 AVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKY---VRKRY 878
Cdd:PRK10841  873 TLPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVYaerVRKSR 924
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
303-681 1.44e-50

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: 184.01  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 303 FGAYRRRLREQN--VAMLGQLYEALSDSIDMAVNLYSPtDGKVTPIVAKAERIIGYRLDAFLqNERLAATIGLSPEGVAL 380
Cdd:COG5000    71 FNRMTDQLKEQReeLEERRRYLETILENLPAGVIVLDA-DGRITLANPAAERLLGIPLEELI-GKPLEELLPELDLAELL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 381 FDRIRKDETkgfEQGEFSFRSKQTgkecwasYSVKRLTFEDKPQLlVVMRDVTadkEIQLSMKdamdvaeaaNAAKSEFL 460
Cdd:COG5000   149 REALERGWQ---EEIELTRDGRRT-------LLVRASPLRDDGYV-IVFDDIT---ELLRAER---------LAAWGELA 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 461 SRMSHEIRTPMNVILGTLQ-----LARSNPDDREKVAETLKKIGDASDHLLGLINDVLDISKIENGKMtlasEPFRLSAV 535
Cdd:COG5000   206 RRIAHEIKNPLTPIQLSAErlrrkLADKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNEL 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 536 LSHVASAVRVQCEQRAQEFVVTTPPcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTV 615
Cdd:COG5000   282 LREVLALYEPALKEKDIRLELDLDP-DLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDG------RVRIEV 354
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 616 SDNGIGMSEEFKEHIFEPF-SmegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNL 681
Cdd:COG5000   355 SDNGPGIPEEVLERIFEPFfT----TKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
437-868 5.36e-50

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 190.83  E-value: 5.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 437 EIQ-----LSMKDAMDvaeaANAAKSEFLSRMSHEIRTPMN-VILGTLQLARS--NPDDREkvaeTLKKIGDASDHLLGL 508
Cdd:PRK11107  273 EIQnveldLAKKRAQE----AARIKSEFLANMSHELRTPLNgVIGFTRQTLKTplTPTQRD----YLQTIERSANNLLAI 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 509 INDVLDISKIENGKMTLASEPFRLSAVLSHVA-----SAvrvqcEQRAQEFVVTTPPCADAVFVGDARRIKQLLLNLLTN 583
Cdd:PRK11107  345 INDILDFSKLEAGKLVLENIPFSLRETLDEVVtllahSA-----HEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGN 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 584 AVKYTPCGGC-VRFETTVAKGAAMgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRS---REQGTGLGMPIVKNIVTMM 659
Cdd:PRK11107  420 AIKFTESGNIdILVELRALSNTKV---QLEVQIRDTGIGISERQQSQLFQAFRQADASisrRHGGTGLGLVITQKLVNEM 496
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 660 AGDIAVESTKGQGTTFTVTFNLRI------------ALEAERI-VFEEGEGA-----------------EADDAQPLE-- 707
Cdd:PRK11107  497 GGDISFHSQPNRGSTFWFHLPLDLnpnpiidglptdCLAGKRLlYVEPNSAAaqatldilsetplevtySPTLSQLPEah 576
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 708 -------LDAASAAALRSLGARDRLA-------------------------------SRPVSAY------EAPMPGAPRA 743
Cdd:PRK11107  577 ydilllgLPVTFREPLTMLHERLAKAksmtdflilalpcheqvlaeqlkqdgadaclSKPLSHTrllpalLEPCHHKQPP 656
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 744 L---DRTEFEGLRVLLAEDNDLNAEIACELLAEagLV--VERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATR 818
Cdd:PRK11107  657 LlppTDESRLPLTVMAVDDNPANLKLIGALLEE--QVehVVLCDSGHQA---VEQAKQRPFDLILMDIQMPGMDGIRACE 731
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2575951464 819 CIRE--LDREdadaVPIIAMSANAFAEDVSASLASGMNAHLSKPID---MRRVLA 868
Cdd:PRK11107  732 LIRQlpHNQN----TPIIAVTAHAMAGERERLLSAGMDDYLAKPIDeamLKQVLL 782
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
308-679 1.53e-48

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: 179.79  E-value: 1.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 308 RRLREQNVAMLGQLYEALSDSIDMAVnLYSPTDGKVTPIVAKAERIIGYRLDAFLqNERLAATIGLSP--EGVALFDRIR 385
Cdd:COG5809   129 RKRMEEALRESEEKFRLIFNHSPDGI-IVTDLDGRIIYANPAACKLLGISIEELI-GKSILELIHSDDqeNVAAFISQLL 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 386 KDETKgfEQGEFSFRSKQtGKECWASYSVKRLTFEDKPQLLVVM-RDVTADKEIQLSMKDAmdvaEAANAAkSEFLSRMS 464
Cdd:COG5809   207 KDGGI--AQGEVRFWTKD-GRWRLLEASGAPIKKNGEVDGIVIIfRDITERKKLEELLRKS----EKLSVV-GELAAGIA 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 465 HEIRTPMNVILGTLQLARSNPDDREKvaETLKKIGDASDHLLGLINDVLDISKIENGKMtlasEPFRLSAVLSHVASAVR 544
Cdd:COG5809   279 HEIRNPLTSLKGFIQLLKDTIDEEQK--TYLDIMLSELDRIESIISEFLVLAKPQAIKY----EPKDLNTLIEEVIPLLQ 352
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 545 VQC-EQRAQ---EFVVTTPPcadavFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTvakgaAMGYRQVKFTVSDNGI 620
Cdd:COG5809   353 PQAlLKNVQielELEDDIPD-----ILGDENQLKQVFINLLKNAIEAMPEGGNITIETK-----AEDDDKVVISVTDEGC 422
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 621 GMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG5809   423 GIPEERLKKLGEPFYT---TKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITL 478
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
273-679 4.18e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 176.13  E-value: 4.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 273 VRAEAAVVTTTFEAVFAIIFACLVVVALLVFGAYRRRLREQNVAMLGQLYEALSDSIDMAVNLYSPTDGKVTPIVAKAER 352
Cdd:COG4251    92 VLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALL 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 353 IIGYRLDAFLQNERLAATIGLSPEGVALFDRIRKDETKGFEQGEFSFRSKQTGKECWASYSVKRLTFEDKPQLLVVMRDV 432
Cdd:COG4251   172 LAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILV 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 433 TADKEIQLSMKDAMDVA-------EAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDR--EKVAETLKKIGDASD 503
Cdd:COG4251   252 LELLELRLELEELEEELeertaelERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKldEEGREYLERIRDAAE 331
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 504 HLLGLINDVLDISKIENGKMTLasEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPcadaVFVGDARRIKQLLLNLLTN 583
Cdd:COG4251   332 RMQALIDDLLAYSRVGRQELEF--EPVDLNELLEEVLEDLEPRIEERGAEIEVGPLP----TVRGDPTLLRQVFQNLISN 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 584 AVKYTPCG--GCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFS-MEGRSREQGTGLGMPIVKNIVTMMA 660
Cdd:COG4251   406 AIKYSRPGepPRIEIGAEREGG------EWVFSVRDNGIGIDPEYAEKIFEIFQrLHSRDEYEGTGIGLAIVKKIVERHG 479
                         410
                  ....*....|....*....
gi 2575951464 661 GDIAVESTKGQGTTFTVTF 679
Cdd:COG4251   480 GRIWVESEPGEGATFYFTL 498
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
430-863 2.44e-44

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 174.15  E-value: 2.44e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  430 RDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAETLKKIGDASDHLLGLI 509
Cdd:PRK09959   686 QDITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSLLGLI 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  510 NDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVGDARRIKQLLLNLLTNAVKYTp 589
Cdd:PRK09959   766 GEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFT- 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  590 CGGCVRFETTVAKgAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQ-GTGLGMPIVKNIVTMMAGDIAVEST 668
Cdd:PRK09959   845 TEGAVKITTSLGH-IDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQtGSGLGLMICKELIKNMQGDLSLESH 923
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  669 KGQGTTFTVTFNLRIaleaerivFEEGEGAEADDAQPLELDaasaaalrslgardrlasrpvsayeapmpgapraldrte 748
Cdd:PRK09959   924 PGIGTTFTITIPVEI--------SQQVATVEAKAEQPITLP--------------------------------------- 956
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  749 fEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDreda 828
Cdd:PRK09959   957 -EKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQA---LHKVSMQHYDLLITDVNMPNMDGFELTRKLREQN---- 1028
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 2575951464  829 DAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDM 863
Cdd:PRK09959  1029 SSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTL 1063
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
463-679 1.25e-40

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 153.42  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 463 MSHEIRTPMNVILGTLQLAR---SNPDDREKVAETLKKIGDASDHLLGLINDVLDISKiengKMTLASEPFRLSAVLSHV 539
Cdd:COG4191   149 IAHEINNPLAAILGNAELLRrrlEDEPDPEELREALERILEGAERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEA 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 540 ASAVRVQCEQRAQEFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTP--CGGCVRFETTVAKGaamgyrQVKFTVSD 617
Cdd:COG4191   225 LELLRPRLKARGIEVELDLPPDLPPVL-GDPGQLEQVLLNLLINAIDAMEegEGGRITISTRREGD------YVVISVRD 297
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 618 NGIGMSEEFKEHIFEPF--SmegRSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG4191   298 NGPGIPPEVLERIFEPFftT---KPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
426-873 3.73e-39

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 156.99  E-value: 3.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 426 LVVMRdvTAD-KEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPdDREKVAETLKKIGDASDH 504
Cdd:PRK11466  415 QVKAR--TAElQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNP-ALNAQRDDLRAITDSGES 491
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 505 LLGLINDVLDISKIENG--KMTLASEPFR----LSAVLSHVASAVRVQCEQRAQEFVVTTPpcadAVFVGDARRIKQLLL 578
Cdd:PRK11466  492 LLTILNDILDYSAIEAGgkNVSVSDEPFEprplLESTLQLMSGRVKGRPIRLATDIADDLP----TALMGDPRRIRQVIT 567
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 579 NLLTNAVKYTPCGG-CVRFETTvakgaamgYRQVKFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGTGLGMPIVKNIVT 657
Cdd:PRK11466  568 NLLSNALRFTDEGSiVLRSRTD--------GEQWLVEVEDSGCGIDPAKLAEIFQPF-VQVSGKRGGTGLGLTISSRLAQ 638
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 658 MMAGDIAVESTKGQGTTFTVTFNLRIALEAERIVFeegegaeaddAQPLELDaasaaalrslgardrlasrpvsayeapm 737
Cdd:PRK11466  639 AMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTV----------NQAVRLD---------------------------- 680
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 738 pgapraldrtefeGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyFDAVLMDVQMPNMNGYeat 817
Cdd:PRK11466  681 -------------GLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNSEP--FAAALVDFDLPDYDGI--- 742
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 818 rcirELDREDADAVP---IIAMSANAFAEDVSASLASGMNAHLSKPIDmRRVLATLIKY 873
Cdd:PRK11466  743 ----TLARQLAQQYPslvLIGFSAHVIDETLRQRTSSLFRGIIPKPVP-REVLGQLLAH 796
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
424-679 2.26e-38

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: 146.20  E-value: 2.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 424 QLLVVMRDVTadkeiQLSMKDAMdvaeaanaaKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAE-TLKKIGDAS 502
Cdd:TIGR02966  96 QKLLVARDVT-----RLRRLEQM---------RRDFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNrALEIMLEQS 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 503 DHLLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTtppCADAVFV-GDARRIKQLLLNLL 581
Cdd:TIGR02966 162 QRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFE---IDGGVDVlGDEDELRSAFSNLV 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 582 TNAVKYTPCGGCVRFE-TTVAKGAamgyrqvKFTVSDNGIGMSEEFKEHIFEPFSM--EGRSREQ-GTGLGMPIVKNIVT 657
Cdd:TIGR02966 239 SNAIKYTPEGGTITVRwRRDGGGA-------EFSVTDTGIGIAPEHLPRLTERFYRvdKSRSRDTgGTGLGLAIVKHVLS 311
                         250       260
                  ....*....|....*....|..
gi 2575951464 658 MMAGDIAVESTKGQGTTFTVTF 679
Cdd:TIGR02966 312 RHHARLEIESELGKGSTFSFIF 333
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
747-877 2.79e-38

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: 138.83  E-value: 2.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 747 TEFEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldRE 826
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIRA--LP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 827 DADAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
754-870 3.28e-37

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: 135.29  E-value: 3.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREDADaVPI 833
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEA---LELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRR-TPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17546    77 IALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
436-684 2.79e-35

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 140.27  E-value: 2.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 436 KEIQLSMKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLAR----SNPDDR--EKVAETLKKIGDasdhllgLI 509
Cdd:COG5808   221 KRKTLLERVIQEINTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQekypELEDQKyfDIIQEEIQRINQ-------IV 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 510 NDVLDISKIENGKMTLASepfrLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTP 589
Cdd:COG5808   294 SEFLVLGKPTAKKLELDD----LNELIEEILSIIDSEANLKNIRVEKQSLDEPLHIK-CDKDRIKQVLLNLIKNAIEAMK 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 590 CGGCVRFETTVAKGAAMgyrqvkFTVSDNGIGMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTK 669
Cdd:COG5808   369 EGGKLTISIENDDEKAV------IEVIDNGEGIPEDIIDEIFEPFVT---TKEGGTGLGLSVCKRIVEMHGGEIDIESEE 439
                         250
                  ....*....|....*
gi 2575951464 670 GQGTTFTVTFNLRIA 684
Cdd:COG5808   440 GKGTTFTIRLPLKKE 454
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
306-682 4.81e-35

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


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 137.22  E-value: 4.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 306 YRRRLREQNVAMLGQ---LYEALSDSIDMAVNLYSpTDGKVTPIVAKAERIIGYRLDAFlqnerlaatIGLSPEGVALFD 382
Cdd:COG5807    10 YHIEEKNQEFKLTEDsefKFKQLFDSILEFVFFID-SKGEILECNDFAEDLYGLSQNEY---------IGKTFVEEKCIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 383 RIRKDETK-GFEQGEFSFRSKQTgkecwASYSVKRLTFEDKPQ---LLVVMRDVTADKEIQlsmkDAMDVAEAANAAKsE 458
Cdd:COG5807    80 KDEQLYNKeAFDRIEISYLTKNG-----EFDEIIYPIYYKDGVilgLITVYRDITKRKEAE----DKLLRSEKLSVAG-E 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPMNVILGTLQL--ARSNPDDREkvaETLKKIGDASDHLLGLINDVLDISKIENGKMtlasEPFRLSAVL 536
Cdd:COG5807   150 LAAGIAHEIRNPLTSIKGFLQLlqESREDSERE---EYFNIIISEIDRINTIITELLVLSKPKKFNF----KKLNLNDVL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 537 SHVASAVRVQCEQRAQEFVVTTPPcaDAVFV-GDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKgaamgyRQVKFTV 615
Cdd:COG5807   223 EDVIALLSTEAILKNISIKYDLAD--DEPVInGDKNQLKQVFINLIKNAIEAMETGGNITIKTYVEG------DFVVISV 294
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 616 SDNGIGMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLR 682
Cdd:COG5807   295 KDEGIGIPEEVLEKIGEPFFT---TKEEGTGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLPLY 358
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
568-682 6.27e-34

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 125.84  E-value: 6.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464  568 GDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSM--EGRSREQGT 645
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD------HVEITVEDNGPGIPPEDLEKIFEPFFRtdKRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2575951464  646 GLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLR 682
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
573-679 1.66e-33

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: 124.25  E-value: 1.66e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE-QGTGLGMPI 651
Cdd:cd00075     1 LEQVLSNLLDNALKYSPPGGTIEISLRQEGD------GVVLEVEDNGPGIPEEDLERIFERFYRGDKSREgGGTGLGLAI 74
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 652 VKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd00075    75 VRRIVEAHGGRITVESEPGGGTTFTVTL 102
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
457-679 5.81e-32

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: 129.22  E-value: 5.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 457 SEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAETLKKIGDASDHLLGLINDVLDISKIENGKMtlasEPFRLSAVL 536
Cdd:COG5806   202 SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKL----EKIDVSEEL 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 537 SHVASAVRVQCEQRAQEFVVTTPPcaDAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVS 616
Cdd:COG5806   278 EHVIDVLSPYANMNNVEIQTELEP--GLYIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKN------KVIISIK 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 617 DNGIGMSEEFKEHIFEP-FSmegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG5806   350 DTGVGMTKEQLERLGEPyFS----TKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITL 409
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
568-683 7.17e-32

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: 119.78  E-value: 7.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 568 GDARRIKQLLLNLLTNAVKYTPCGGCVRFetTVAKGAamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGTGL 647
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITV--TLSEGG-----ELTLTVEDNGIGIPPEDLPRIFEPFSTADKRGGGGTGL 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 648 GMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLRI 683
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
573-681 2.76e-31

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: 117.98  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTPcGGCVRFETTVAKGAAMGYrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRS---REQGTGLGM 649
Cdd:cd16922     1 LRQILLNLLGNAIKFTE-EGEVTLRVSLEEEEEDGV-QLRFSVEDTGIGIPEEQQARLFEPFSQADSSttrKYGGTGLGL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2575951464 650 PIVKNIVTMMAGDIAVESTKGQGTTFTVTFNL 681
Cdd:cd16922    79 AISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
752-875 9.50e-28

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: 110.38  E-value: 9.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDRedADAV 831
Cdd:COG3706     2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR---PDLILLDLEMPDMDGLELCRRLRADPR--TADI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVR 875
Cdd:COG3706    77 PIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVAR 120
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
310-679 8.99e-27

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: 115.21  E-value: 8.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 310 LREQNvamlgQLYEALSDSIDMAVNLYSpTDGKVTPIVAKAERIIGYRLDAFLQNERLAatIGLSPEGVALFDRIRKDeT 389
Cdd:COG5805   152 LQEQE-----ERLQTLIENSPDLICVID-TDGRILFINESIERLFGAPREELIGKNLLE--LLHPCDKEEFKERIESI-T 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 390 KGFEQGEF--SFRSKQtGKECW--ASYSVKRLTFEDKPQLLVVMRDVTADKEIQLSMkdamdvaeaanaAKSEFLS---R 462
Cdd:COG5805   223 EVWQEFIIerEIITKD-GRIRYfeAVIVPLIDTDGSVKGILVILRDITEKKEAEELM------------ARSEKLSiagQ 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 463 MS----HEIRTPMNVILGTLQLARSNPDDREKVAETlkkIGDASDHLLGLINDVLDISKiengKMTLASEPFRLSAVLSH 538
Cdd:COG5805   290 LAagiaHEIRNPLTSIKGFLQLLQPGIEDKEEYFDI---MLSELDRIESIISEFLALAK----PQAVNKEKENINELIQD 362
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 539 VAS-----AVRVQCEQRAQEFVVttppcaDAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAkgaamgYRQVKF 613
Cdd:COG5805   363 VVTlleteAILHNIQIRLELLDE------DPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEE------DNSVII 430
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:COG5805   431 RVIDEGIGIPEERLKKLGEPFFT---TKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITL 493
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
753-869 1.27e-26

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: 104.93  E-value: 1.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRElDREDADaVP 832
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEK---PDLILMDIQLPGMDGLEATRLLKE-DPATRD-IP 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLAT 869
Cdd:cd17548    76 VIALTAYAMKGDREKILEAGCDGYISKPIDTREFLET 112
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
271-679 5.61e-26

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 113.91  E-value: 5.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 271 ENVRAEAAVVTTtfeAVFAIIFAcLVVVALLVFGAYRRRLrEQNVAM----------------------LGQ-------L 321
Cdd:PRK11360  179 EDIRRQAWKMDR---RIYAVLAA-GLVIGLLLIFLLSRRF-SANVDIikdglstlendlstrlpplpgeLGEisqainnL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 322 YEALSD----------SID---MAVNlyspTDGKVTPIVAKAERIIGYRLDAFLQNERLAATIGLSPEGVALFDRIRKDE 388
Cdd:PRK11360  254 AQALREtrslnelileSIAdgvIAID----RQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASPLLDTLEHGT 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 389 T-KGFEqgeFSFRSKQTGKECWASYSVKRLTFEDKPQLLVVMRDVTADKEIQLSMKDAMDVAeaanaAKSEFLSRMSHEI 467
Cdd:PRK11360  330 EhVDLE---ISFPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQERLA-----ALGELVAGVAHEI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 468 RTPMNVILGTLQLARSNPDD---REKVAETLKKIgdasDHLLGLINDVLDISKIENGKMtlasEPFRLSAVLSHVASAVR 544
Cdd:PRK11360  402 RNPLTAIRGYVQIWRQQTSDppsQEYLSVVLREV----DRLNKVIDQLLEFSRPRESQW----QPVSLNALVEEVLQLFQ 473
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 545 VQCEQRAQEFVVTTPPCADAVFVgDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyRQVKFTVSDNGIGMSE 624
Cdd:PRK11360  474 TAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQAISARGKIRIRTWQYSD-----GQVAVSIEDNGCGIDP 547
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2575951464 625 EFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:PRK11360  548 ELLKKIFDPFFT---TKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYL 599
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
752-870 4.74e-25

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: 103.50  E-value: 4.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldreDADAV 831
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER---PDLILLDLMLPGMDGLEVCRRLRA----RPSDI 74
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:COG0745    75 PIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
459-677 7.74e-24

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 107.84  E-value: 7.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAETLKKIGDASDHLLGLINDVLDISKiengKMTLASEPFRLSAVLSH 538
Cdd:PRK13837  453 LASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTE 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 539 VASAVRVQCEQRAqEFVVTTPPcADAVFVGDARRIKQLLLNLLTNA---------VKYTPCGGCVRFETTVAKGAAMGYR 609
Cdd:PRK13837  529 IAPLLRVSLPPGV-ELDFDQDQ-EPAVVEGNPAELQQVLMNLCSNAaqamdgagrVDISLSRAKLRAPKVLSHGVLPPGR 606
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575951464 610 QVKFTVSDNGIGMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:PRK13837  607 YVLLRVSDTGAGIDEAVLPHIFEPFFT---TRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDV 671
PRK09303 PRK09303
histidine kinase;
455-678 8.80e-24

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 104.26  E-value: 8.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 455 AKSEFLSRMSHEIRTPM---NVILGTLQLARSNPDDREKVAET----------LKKIGDasdhllgLINDVLDISKIENG 521
Cdd:PRK09303  150 FKDRVLAMLAHDLRTPLtaaSLALETLELGQIDEDTELKPALIeqlqdqarrqLEEIER-------LITDLLEVGRTRWE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 522 KMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTPCGGCVRFettva 601
Cdd:PRK09303  223 ALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVY-ADQERIRQVLLNLLDNAIKYTPEGGTITL----- 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 602 kgaAMGYR---QVKFTVSDNGIGMSEEFKEHIFepfsmEGR---SREQGT---GLGMPIVKNIVTMMAGDIAVESTKGQG 672
Cdd:PRK09303  297 ---SMLHRttqKVQVSICDTGPGIPEEEQERIF-----EDRvrlPRDEGTegyGIGLSVCRRIVRVHYGQIWVDSEPGQG 368

                  ....*.
gi 2575951464 673 TTFTVT 678
Cdd:PRK09303  369 SCFHFT 374
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
464-677 4.25e-23

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 103.71  E-value: 4.25e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 464 SHEIRTPMNVILGTL----QLARSNPDDREkVAETLKKigdASDHLLGLINDVLDISKIENgkmtLASEPFRLSAVLSHV 539
Cdd:PRK10364  245 AHEIRNPLSSIKGLAkyfaERAPAGGEAHQ-LAQVMAK---EADRLNRVVSELLELVKPTH----LALQAVDLNDLINHS 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 540 ASAVRVQCEQRAQEFVVTTPPCADAVFVgDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKgaamgyRQVKFTVSDNG 619
Cdd:PRK10364  317 LQLVSQDANSREIQLRFTANDTLPEIQA-DPDRLTQVLLNLYLNAIQAIGQHGVISVTASESG------AGVKISVTDSG 389
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2575951464 620 IGMSEEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:PRK10364  390 KGIAADQLEAIFTPYFT---TKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTL 444
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
287-682 4.91e-23

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 102.23  E-value: 4.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 287 VFAIIFACLVVVALLVFGAYRRRLREQNVAMLGQlYEALSDSIDMAVNLYSpTDGKVTPIVAKAERIIGyrldaflqner 366
Cdd:COG3290    52 LLLILLLILLLLLLLLLAALLLKLLEEIARLVEE-REAVLESIREGVIAVD-RDGRITLINDAARRLLG----------- 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 367 laatigLSPEGVALFDRIRKDETKGFEQGEFSFRSKqtgkecWASYSVKRLTFEDKPQLLVV-MRDVTadkEIQLSMKDA 445
Cdd:COG3290   119 ------LDAIGRPIDEVLAEVLETGERDEEILLNGR------VLVVNRVPIRDDGRVVGAVAtFRDRT---ELERLEEEL 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 446 MDVAEAANAaksefLSRMSHEIRTPMNVILGTLQLARSnpddrEKVAETLKKIGDASDHLLGLI-----NDVLDIskIEN 520
Cdd:COG3290   184 EGVKELAEA-----LRAQRHDFRNHLHTISGLLQLGEY-----DEALEYIDEISEELQELIDSLlsrigNPVLAA--LLL 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 521 GKMTLASEpfrlsavlSHVAsaVRVQCEQRaqefvVTTPPCADAVFVgdarrikQLLLNLLTNAV----KYTPCGGCVRF 596
Cdd:COG3290   252 GKAARARE--------RGID--LTIDIDSD-----LPDLPLSDTDLV-------TILGNLLDNAIeaveKLPEEERRVEL 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 597 ETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPfsmeGRS--REQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTT 674
Cdd:COG3290   310 SIRDDGD------ELVIEVEDSGPGIPEELLEKIFER----GFStkLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTV 379

                  ....*...
gi 2575951464 675 FTVTFNLR 682
Cdd:COG3290   380 FTVRLPKE 387
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
457-679 7.72e-23

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: 102.85  E-value: 7.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 457 SEFLSRMSHEIRTPMNVILGTLQLA----RSNPDDREKVAETLKKIgdasDHLLGLINDVLDISKIENGKMTLASEPFRL 532
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVAlsqpRTGEEYREVLESNLEEL----ERLSRMVSDMLFLARADNGQLALERVRLDL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 533 SAVLSHVASAVRVQCEQRAQEFVVTtppcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAamgyrqVK 612
Cdd:TIGR01386 318 AAELAKVAEYFEPLAEERGVRIRVE----GEGLVRGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDE------VR 387
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 613 FTVSDNGIGMSEEFKEHIFEPFSMEGRSR---EQGTGLGMPIVKNIVTMMAGDIAVESTKGQgTTFTVTF 679
Cdd:TIGR01386 388 VSVSNPGPGIPPEHLSRLFDRFYRVDPARsnsGEGTGLGLAIVRSIMEAHGGRASAESPDGK-TRFILRF 456
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
424-688 8.95e-23

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 102.01  E-value: 8.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 424 QLLVVMRDVTADKEIQlsmkdamdvaeaanAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDD---REKVAETLKkigD 500
Cdd:PRK11006  186 QLLMVARDVTQMHQLE--------------GARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEgalREKALHTMR---E 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 501 ASDHLLGLINDVLDISKIENGKMTLASE----PFRLSaVLSHVASAVrvqcEQRAQEFVVTTPPcADAVFvGDARRIKQL 576
Cdd:PRK11006  249 QTQRMEGLVKQLLTLSKIEAAPTIDLNEkvdvPMMLR-VLEREAQTL----SQGKHTITFEVDN-SLKVF-GNEDQLRSA 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 577 LLNLLTNAVKYTPCGG--CVRFETTvAKGAamgyrqvKFTVSDNGIGMSEEFKEHIFEPFSM--EGRSREQG-TGLGMPI 651
Cdd:PRK11006  322 ISNLVYNAVNHTPEGThiTVRWQRV-PQGA-------EFSVEDNGPGIAPEHIPRLTERFYRvdKARSRQTGgSGLGLAI 393
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2575951464 652 VKNIVTMMAGDIAVESTKGQGTTFTVTFNLRIALEAE 688
Cdd:PRK11006  394 VKHALSHHDSRLEIESEVGKGTRFSFVLPERLIAKNS 430
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
754-870 1.39e-22

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: 93.37  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDredaDAVPI 833
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---PDLILLDINMPGMDGLELLKRIRRRD----PTTPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
754-870 1.51e-22

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: 93.29  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldREDADAVPI 833
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR---PDVILSDIGMPGMDGYELARRLRE--LPWLANTPA 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17580    76 IALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
747-877 7.10e-22

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: 95.23  E-value: 7.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 747 TEFEGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldRE 826
Cdd:COG3437     2 RTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP---PDLILLDVRMPGMDGFELLRLLRA--DP 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 827 DADAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG3437    77 STRDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
752-877 1.01e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 88.87  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGL--VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdad 829
Cdd:COG4565     4 IRVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRP---DLILLDIYLPDGDGLELLRELRARGPD--- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2575951464 830 aVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG4565    78 -VDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYR 124
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
755-860 1.28e-20

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: 87.28  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 755 LLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREdadaVPII 834
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEA---LELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD----IPVI 73
                          90       100
                  ....*....|....*....|....*.
gi 2575951464 835 AMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd00156    74 VLTAKADEEDAVRALELGADDYLVKP 99
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
456-679 2.63e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.89  E-value: 2.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 456 KSEFLSRMSHEIRTPMNVILGTLQLARS--NPDDREKVAETLKKIGDasdhLLGLINDVLDISKIENGKMTLASEPFRLS 533
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAIQDgiRKFTPESLDSLQAEVGT----LTKLVDDLHDLSMSDEGALAYQKASVDLV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 534 AVLSHVASAVRVQCEQRAQEFVVTTPpcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFEttvakgAAMGYRQVKF 613
Cdd:NF012163  316 PLLEVEGGAFRERFASAGLELEVSLP--DSSLVFGDRDRLMQLFNNLLENSLRYTDSGGSLHIS------ASQRPKEVTL 387
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:NF012163  388 TVADSAPGVSDEQLARLFERFYRVEVSRNRasgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTL 456
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
459-678 5.74e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 94.32  E-value: 5.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPmnviLGTLQLARSN-PDDREKV-------AETLKKIGDASDHLLgliNDVLDISKIENGKMTLASEPF 530
Cdd:NF040691  274 FVSDVSHELRTP----LTTIRMAADViHDSRDDFdpatarsAELLHTELDRFESLL---SDLLEISRFDAGAAELDVEPV 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 531 RLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVgDARRIKQLLLNLLTNAVKYtpcGGCVRFETTVakgaAMGYRQ 610
Cdd:NF040691  347 DLRPLVRRVVDALRQLAERAGVELRVDAPGTPVVAEV-DPRRVERVLRNLVVNAIEH---GEGKPVVVTV----AQDDTA 418
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 611 VKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:NF040691  419 VAVTVRDHGVGLKPGEVALVFDRFWRADPARARttgGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-678 5.63e-19

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: 82.76  E-value: 5.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTpcggcvrfETTVAKGAAMGYRQV----KFTVSDNGIGMSEEFKEHIFEPFS-MEGRSREQGTGL 647
Cdd:cd16921     1 LGQVLTNLLGNAIKFR--------RPRRPPRIEVGAEDVgeewTFYVRDNGIGIDPEYAEKVFGIFQrLHSREEYEGTGV 72
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2575951464 648 GMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16921    73 GLAIVRKIIERHGGRIWLESEPGEGTTFYFT 103
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
463-682 5.71e-19

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 91.06  E-value: 5.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 463 MSHEIRTPMNVILGTLQLARSN--PDDREKVAETlkkIGDASDHLLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVA 540
Cdd:PRK11100  263 LTHELKSPLAAIRGAAELLQEDppPEDRARFTGN---ILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELV 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 541 SAVRVQCEQRAQEFVVTTPpcaDAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGI 620
Cdd:PRK11100  340 EAREAQAAAKGITLRLRPD---DARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGE------QVALSVEDQGP 410
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 621 GMSEEFKEHIFEPFSMEGR--SREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLR 682
Cdd:PRK11100  411 GIPDYALPRIFERFYSLPRpaNGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPRH 474
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
750-877 1.06e-18

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: 89.64  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDREdad 829
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEP---PDLVLLDLRMPGMDGLELLRELRALDPD--- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2575951464 830 aVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG2204    75 -LPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
453-517 1.07e-17

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: 78.02  E-value: 1.07e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2575951464 453 NAAKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKVAETLKKIGDASDHLLGLINDVLDISK 517
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
455-521 1.21e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 77.64  E-value: 1.21e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 455 AKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDrEKVAETLKKIGDASDHLLGLINDVLDISKIENG 521
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLD-EEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
569-677 1.95e-17

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: 78.69  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamGYRQVkfTVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GT 645
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRL---NRFLL--TVSDSGPGIPPNLREEIFERFRQGDGSSTRahgGT 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2575951464 646 GLGMPIVKNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:cd16925    76 GLGLSIVKEFVELHGGTVTVSDAPGGGALFQV 107
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-677 6.88e-17

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: 77.08  E-value: 6.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTPCGGCVRFETtvakgaAMGYRQVKFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGTGLGMPIV 652
Cdd:cd16943     4 LNQVLLNLLVNAAQAMEGRGRITIRT------WAHVDQVLIEVEDTGSGIDPEILGRIFDPF-FTTKPVGEGTGLGLSLS 76
                          90       100
                  ....*....|....*....|....*
gi 2575951464 653 KNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:cd16943    77 YRIIQKHGGTIRVASVPGGGTRFTI 101
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
575-679 7.92e-17

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: 77.03  E-value: 7.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 575 QLLLNLLTNAVKYTPCGGCVRFET---TVAKGAAMGYRQ------VKFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGT 645
Cdd:cd16919     3 LAILNLAVNARDAMPEGGRLTIETsnqRVDADYALNYRDlipgnyVCLEVSDTGSGMPAEVLRRAFEPF-FTTKEVGKGT 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2575951464 646 GLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16919    82 GLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYL 115
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
751-874 8.51e-17

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 77.14  E-value: 8.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 751 GLRVLLaedndlnaeiaCELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdada 830
Cdd:COG5803    13 GIRMLL-----------KEVLKKEGYEVFQAANGKEALEKVKELKP---DLVLLDMKMPGMDGIEILKEIKEIDPD---- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYV 874
Cdd:COG5803    75 IPVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
460-657 1.08e-16

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 83.83  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 460 LSRMSHEIRTPmnviLGTLQLA-----RSNPDDREkvaetLKKIGDASDHLLGLINDVLDISKIENgKMTLASEPFRLSA 534
Cdd:PRK09470  247 LSDISHELRTP----LTRLQLAtallrRRQGESKE-----LERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANS 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 535 VLSHVASAVRVQCEQRAQEFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTpcggcvrfETTVAKGAAMGYRQVKFT 614
Cdd:PRK09470  317 LWSEVLEDAKFEAEQMGKSLTVSAPPGPWPIN-GNPNALASALENIVRNALRYS--------HTKIEVAFSVDKDGLTIT 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2575951464 615 VSDNGIGMSEEFKEHIFEPF--SMEGRSREQ-GTGLGMPIVKNIVT 657
Cdd:PRK09470  388 VDDDGPGVPEEEREQIFRPFyrVDEARDRESgGTGLGLAIVENAIQ 433
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
751-870 1.16e-16

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: 79.23  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 751 GLRVLLAEDNDLNAEIACELLAEAG-LVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIREldredAD 829
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRELK---PDLVIVDIDMPDRDGLEAARQISE-----ER 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2575951464 830 AVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:COG3707    75 PAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
PRK10490 PRK10490
sensor protein KdpD; Provisional
460-694 2.01e-16

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 84.32  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 460 LSRMSHEIRTPMNVILG-----TLQLArsnpddrekvAETLKKIGDASD---HLLG---LINDVLDISKIENGKMTLASE 528
Cdd:PRK10490  668 LAALSHDLRTPLTVLFGqaeilTLDLA----------SEGSPHARQASEirqQVLNttrLVNNLLDMARIQSGGFNLRKE 737
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 529 PFRLSAVlshVASAVRVQCEQRAQEFVVTTPPcADAVFV-GDARRIKQLLLNLLTNAVKYTpcGGCvrfeTTVAKGAAMG 607
Cdd:PRK10490  738 WLTLEEV---VGSALQMLEPGLSGHPINLSLP-EPLTLIhVDGPLFERVLINLLENAVKYA--GAQ----AEIGIDAHVE 807
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 608 YRQVKFTVSDNGIGMSEEFKEHIFEPFSmegRSREQ----GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLRI 683
Cdd:PRK10490  808 GERLQLDVWDNGPGIPPGQEQLIFDKFA---RGNKEsaipGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLET 884
                         250
                  ....*....|.
gi 2575951464 684 ALEAERIVFEE 694
Cdd:PRK10490  885 PPELEEFHEDM 895
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
455-521 3.31e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 73.75  E-value: 3.31e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464  455 AKSEFLSRMSHEIRTPMNVILGTLQLARSNPDDREKvAETLKKIGDASDHLLGLINDVLDISKIENG 521
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQ-REYLETILREAERLLRLINDLLDLSRIEAG 66
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
459-678 4.36e-16

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: 82.87  E-value: 4.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPMNVILGTLQLARSNPDDREKvAETLKKIGDASDHLLGLINDVLDISKIENGKMTLASEPFRLSAVLSH 538
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEK-QKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSG 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 539 VASAVRVQCEQRAQEFVVTTPPCadaVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAMgyrqvkFTVSDN 618
Cdd:TIGR03785 567 CMQGYQMTYPPQRFELNIPETPL---VMRGSPELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKSHAL------LTVSNE 637
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 619 GIGMSEEFKEHIFEPF---SMEGRSREQGTGLGMPIVKNIVTMMAGDIAVEST-KGQGTTFTVT 678
Cdd:TIGR03785 638 GPPLPEDMGEQLFDSMvsvRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRqQNDGVVFRIS 701
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
755-860 5.58e-16

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: 73.98  E-value: 5.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 755 LLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREdadaVPII 834
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEA---LELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD----IPII 73
                          90       100
                  ....*....|....*....|....*.
gi 2575951464 835 AMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd17574    74 MLTAKDEEEDKVLGLELGADDYITKP 99
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
568-679 6.82e-16

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: 74.36  E-value: 6.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 568 GDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAMgyrqvkfTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGTGL 647
Cdd:cd16940     9 GDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVI-------RVEDNGPGIDEEELEALFERFYRSDGQNYGGSGL 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2575951464 648 GMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16940    82 GLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
753-860 1.00e-15

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: 73.65  E-value: 1.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAG--LVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdada 830
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKP---DLVITDINMPGMDGLELLEAIRELDPD---- 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:COG4753    74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
PRK13557 PRK13557
histidine kinase; Provisional
449-822 7.24e-15

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 78.56  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 449 AEAA--NAAKSEFLSRM----SHEIRTPMNVILG---TLQLARSNPD-DREKVAETLKKIGDASDHLLGLINDVLDISKi 518
Cdd:PRK13557  150 AEDAlrQAQKMEALGQLtggiAHDFNNLLQVMSGyldVIQAALSHPDaDRGRMARSVENIRAAAERAATLTQQLLAFAR- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 519 engKMTLASEPFRLSAVLSHVASAVR------VQCEQRAQEFVvttPPCadavfvgdarRIKQL-----LLNLLTNAVKY 587
Cdd:PRK13557  229 ---KQRLEGRVLNLNGLVSGMGELAErtlgdaVTIETDLAPDL---WNC----------RIDPTqaevaLLNVLINARDA 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 588 TPCGGCVRFET---TVAKGAAMGY------RQVKFTVSDNGIGMSEEFKEHIFEPF---SMEGrsreQGTGLGMPIVKNI 655
Cdd:PRK13557  293 MPEGGRVTIRTrnvEIEDEDLAMYhglppgRYVSIAVTDTGSGMPPEILARVMDPFfttKEEG----KGTGLGLSMVYGF 368
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 656 VTMMAGDIAVESTKGQGTTFtvtfnlrialeaeRIVFEEGEGAEADDAQPleldaasaaalrslgardrlasrpvsayea 735
Cdd:PRK13557  369 AKQSGGAVRIYSEVGEGTTV-------------RLYFPASDQAENPEQEP------------------------------ 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 736 pmpgAPRALDRTEFEglRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASkiGYFDAVLMDVQMP-NMNGY 814
Cdd:PRK13557  406 ----KARAIDRGGTE--TILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSH--PEVDLLFTDLIMPgGMNGV 477

                  ....*...
gi 2575951464 815 EATRCIRE 822
Cdd:PRK13557  478 MLAREARR 485
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-678 7.32e-15

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: 71.27  E-value: 7.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAmGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMegrSREQGTGLGMPIV 652
Cdd:cd16920     1 IQQVLINLVRNGIEAMSEGGCERRELTIRTSPA-DDRAVTISVKDTGPGIAEEVAGQLFDPFYT---TKSEGLGMGLSIC 76
                          90       100
                  ....*....|....*....|....*.
gi 2575951464 653 KNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16920    77 RSIIEAHGGRLSVESPAGGGATFQFT 102
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
568-678 9.81e-15

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: 71.39  E-value: 9.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 568 GDARRIKQLLLNLLTNAVKYtpcGGCVRFettvaKGAAMGYRQ--VKFTVSDNGIGMSEEFKEHIFE-PFSMEG--RSRE 642
Cdd:cd16947    16 ANTEALQRILKNLISNAIKY---GSDGKF-----LGMTLREDEkhVYIDIWDKGKGISETEKDHVFErLYTLEDsrNSAK 87
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 643 QGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16947    88 QGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVT 123
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
565-678 1.31e-14

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: 71.34  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 565 VFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAM---------------GYRQVKFTVSDNGIGmsEEFKEH 629
Cdd:cd16938     4 VVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFLEGGSEDrsdrdwgpwrpsmsdESVEIRFEVEINDSG--SPSIES 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 630 IFEPFSMEGRS--REQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16938    82 ASMRNSLNRRYnlSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLL 132
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
750-876 1.82e-14

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: 70.23  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDNDLNaeiacellaeaglVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDRedad 829
Cdd:cd17535    12 EGLRRLLESEPDIE-------------VVGEAADGEEALALLRELR---PDVVLMDLSMPGMDGIEALRRLRRRYP---- 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2575951464 830 AVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMrrvlATLIKYVRK 876
Cdd:cd17535    72 DLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSP----EELIEAIRA 114
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
753-873 2.16e-14

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: 70.52  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVE--RAGDGAEACVMF----EASKIGYFDAVLMDVQMPNMNGYEATRCIREldRE 826
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVPNElhVVRDGEEALDFLrgegEYADAPRPDLILLDLNMPRMDGFEVLREIKA--DP 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2575951464 827 DADAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDM---RRVLATLIKY 873
Cdd:cd17557    79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFeefVEAIRSLGEY 128
PRK10604 PRK10604
sensor protein RstB; Provisional
454-676 2.25e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.18  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 454 AAKSEFLSRMSHEIRTPMnVILgTLQLARS-NPDDREKVAetlkkIGDASDHLLGLINDVLDISKIENGKMTLASEPFRL 532
Cdd:PRK10604  210 ASKKQLIDGIAHELRTPL-VRL-RYRLEMSdNLSAAESQA-----LNRDIGQLEALIEELLTYARLDRPQNELHLSEPDL 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 533 SAVLSHVASAVRVQCEQRaqEFVVTTPPCADaVFVGDARRIKQLLLNLLTNAVKYtpCGGCVRFETTVAKGaamgyrQVK 612
Cdd:PRK10604  283 PAWLSTHLADIQAVTPEK--TVRLDTPHQGD-YGALDMRLMERVLDNLLNNALRY--AHSRVRVSLLLDGN------QAC 351
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 613 FTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGT---GLGMPIVKNIVTMMAGDIAVESTKGQGTTFT 676
Cdd:PRK10604  352 LIVEDDGPGIPPEERERVFEPFVRLDPSRDRATggcGLGLAIVHSIALAMGGSVNCDESELGGARFS 418
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
569-679 2.53e-14

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: 69.80  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGCVRFEttvakgAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQ---GT 645
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIR------AAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRasgGS 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2575951464 646 GLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16946    75 GLGLAICHNIALAHGGTISAEHSPLGGLRLVLTL 108
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
569-680 6.10e-14

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: 68.85  E-value: 6.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPF--SMEGRSREQGTG 646
Cdd:cd16948     2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSETNEQ------GVVLSIKDFGIGIPEEDLPRVFDKGftGENGRNFQESTG 75
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2575951464 647 LGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFN 680
Cdd:cd16948    76 MGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
755-868 1.18e-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: 68.02  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 755 LLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEAtrcIRELdREDADAVPII 834
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEG---LEYALSGIYDLIILDIMLPGMDGLEV---LKSL-REEGIETPVL 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2575951464 835 AMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17625    74 LLTALDAVEDRVKGLDLGADDYLPKPFSLAELLA 107
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
459-688 1.53e-13

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 73.90  E-value: 1.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPMNVILGTLQLARsnpdD--REKVAETLKKIGDASDHLLGLINDVLDISKIENGKMTLASEPFRLSAVL 536
Cdd:PRK10549  243 FMADISHELRTPLAVLRGELEAIQ----DgvRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALAYRKTPVDLVPLL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 537 SHVASAVRVQCEQRAQEFVVTTPPcaDAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETtvakgaamGYRQVKFTV- 615
Cdd:PRK10549  319 EVAGGAFRERFASRGLTLQLSLPD--SATVFGDPDRLMQLFNNLLENSLRYTDSGGSLHISA--------EQRDKTLRLt 388
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 616 -SDNGIGMSEEFKEHIFEPFSMEGRSREQ---GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLRIALEAE 688
Cdd:PRK10549  389 fADSAPGVSDEQLQKLFERFYRTEGSRNRasgGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVELPLERDLQRE 465
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-677 1.86e-13

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: 67.43  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTP-CGGCVRFETTVAKGAAMG---YRQV-KFTVSDNGIGMSEEFKEHIFEPFSmegRSREQGTGL 647
Cdd:cd16918     1 LIQVFLNLVRNAAQALAgSGGEIILRTRTQRQVTLGhprHRLAlRVSVIDNGPGIPPDLQDTIFYPMV---SGRENGTGL 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 2575951464 648 GMPIVKNIVTMMAGDIAVESTKGQgTTFTV 677
Cdd:cd16918    78 GLAIAQNIVSQHGGVIECDSQPGH-TVFSV 106
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
753-861 1.93e-13

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: 67.14  E-value: 1.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRElDREDADaVP 832
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELP---DLILLDVMMPGMDGFEVCRRLKE-DPETRH-IP 75
                          90       100
                  ....*....|....*....|....*....
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPI 861
Cdd:cd17538    76 VIMITALDDREDRIRGLEAGADDFLSKPI 104
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
579-679 3.11e-13

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: 66.84  E-value: 3.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 579 NLLTNAVKYTPCGGCVRFE-TTVAKGAamgyrqvKFTVSDNGIGMSEEFKEHIFEPF---SMEGRSREQGTGLGMPIVKN 654
Cdd:cd16952     7 NLVSNAVKYTPPSDTITVRwSQEESGA-------RLSVEDTGPGIPPEHIPRLTERFyrvDIERCRNTGGTGLGLAIVKH 79
                          90       100
                  ....*....|....*....|....*
gi 2575951464 655 IVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16952    80 VMSRHDARLLIASELGKGSRFTCLF 104
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
456-678 3.51e-13

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 72.88  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 456 KSEFLSRMSHEIRTPM-NVILGT---LQLARSNPDDREKVAETLKKIGDASDhllgLINDVLDISKIENGKMTLASEPFR 531
Cdd:PRK09835  262 QSNFSADIAHEIRTPItNLITQTeiaLSQSRSQKELEDVLYSNLEELTRMAK----MVSDMLFLAQADNNQLIPEKKMLD 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 532 LSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAvfvGDARRIKQLLLNLLTNAVKYTPCGGC--VRFETTVakgaamgyR 609
Cdd:PRK09835  338 LADEVGKVFDFFEAWAEERGVELRFVGDPCQVA---GDPLMLRRAISNLLSNALRYTPAGEAitVRCQEVD--------H 406
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 610 QVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE---QGTGLGMPIVKNIVTMMAGDIAVEStKGQGTTFTVT 678
Cdd:PRK09835  407 QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQrkgEGSGIGLAIVKSIVVAHKGTVAVTS-DARGTRFVIS 477
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
754-874 5.26e-13

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: 66.20  E-value: 5.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldREDADAVPI 833
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRP---TLVISDIVMPEMDGYELCRKIKS--DPDLKDIPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDmRRVLATLIKYV 874
Cdd:cd17598    76 ILLTTLSDPRDVIRGLECGADNFITKPYD-EKYLLSRIKYI 115
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
753-868 2.26e-12

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: 64.39  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLV-VERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDREdaDAV 831
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLeVVSFTDPREALAWCRENP---PDLILLDYMMPGMDGLEFIRRLRALPGL--EDV 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17551    77 PIVMITADTDREVRLRALEAGATDFLTKPFDPVELLA 113
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
579-672 2.93e-12

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: 63.88  E-value: 2.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 579 NLLTNAVKYTPcggcvrfeTTVAKGAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPF--SMEGRSREQ-GTGLGMPIVKNI 655
Cdd:cd16949     7 NVLRNALRYSP--------SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFyrVDSARDRESgGTGLGLAIAERA 78
                          90
                  ....*....|....*..
gi 2575951464 656 VTMMAGDIAVESTKGQG 672
Cdd:cd16949    79 IEQHGGKIKASNRKPGG 95
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
752-867 3.23e-12

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: 63.96  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEaCVMFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELdREDADAV 831
Cdd:cd19933     1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEE-CLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKL-FGRRERP 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPI---DMRRVL 867
Cdd:cd19933    79 LIVALTANTDDSTREKCLSLGMNGVITKPVslhALGDEL 117
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
750-862 4.33e-12

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: 63.39  E-value: 4.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDndlnaeiacelLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDREdad 829
Cdd:cd17554    10 ENIRELYKEE-----------LEDEGYEVVTAGNGEEALEKLESED---PDLVILDIKMPGMDGLETLRKIREKKPD--- 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2575951464 830 aVPIIAMSANAFAEDVSASLASGMNAHLSKPID 862
Cdd:cd17554    73 -LPVIICTAYSEYKSDFSSWAADAYVVKSSDLT 104
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
752-877 4.93e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 66.76  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAG--LVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdad 829
Cdd:COG3279     2 MKILIVDDEPLARERLERLLEKYPdlEVVGEASNGEEALELLEEHKP---DLVFLDIQMPGLDGFELARQLRELDPP--- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 830 aVPIIAMSA------NAFaeDVSASlasgmnAHLSKPIDMRRVLATLIKYVRKR 877
Cdd:COG3279    76 -PPIIFTTAydeyalEAF--EVNAV------DYLLKPIDEERLAKALEKAKERL 120
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
569-679 5.03e-12

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: 63.25  E-value: 5.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGcvrfetTVAKGAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGT--G 646
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGG------TVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhyG 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2575951464 647 LGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16975    75 MGLYIAKNLVEKHGGSLIIENSQKGGAEVTVKI 107
PRK10337 PRK10337
sensor protein QseC; Provisional
459-655 5.14e-12

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 68.91  E-value: 5.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPM---NVILGTLQLARSNPDDREKvaeTLKKIGDASDHLLGLINDVLDISKIENGKMTLASEPFRL--- 532
Cdd:PRK10337  240 FTSDAAHELRSPLaalKVQTEVAQLSDDDPQARKK---ALLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLedl 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 533 --SAVLSHVASAVRVQCEQRAQefVVTTPPCadavfvgdaRRIKQLLL-----NLLTNAVKYTPCGGCVRFeTTVAKGaa 605
Cdd:PRK10337  317 lqSAVMDIYHTAQQAGIDVRLT--LNAHPVI---------RTGQPLLLsllvrNLLDNAIRYSPQGSVVDV-TLNARN-- 382
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2575951464 606 mgyrqvkFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGTGLGMPIVKNI 655
Cdd:PRK10337  383 -------FTVRDNGPGVTPEALARIGERFYRPPGQEATGSGLGLSIVRRI 425
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
754-870 1.75e-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: 61.73  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIreldREDADAVPI 833
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEA---EAALASGPYDLVILDLGLPDGDGLDLLRRW----RRQGQSLPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17624    74 LILTARDGVDDRVAGLDAGADDYLVKPFALEELLARL 110
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
753-863 2.11e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 67.18  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRedadAVP 832
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP---DVVLMDIRMPEMDGIKALKEMRSHET----RTP 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDM 863
Cdd:PRK11361   79 VILMTAYAEVETAVEALRCGAFDYVIKPFDL 109
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
753-872 2.50e-11

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: 61.53  E-value: 2.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGL-VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdadaV 831
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYeVVGEAANGEEAVEKYKELKP---DLVTMDITMPEMDGIEALKEIKKIDPN----A 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIK 872
Cdd:cd17542    75 KVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEK 115
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
569-679 3.02e-11

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: 61.01  E-value: 3.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAMGYRQVkFTVSDNGIGMSEEFKEHIFEPFSMegrSREQGTGLG 648
Cdd:cd16944     1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRIRVEADQDGRIV-LIVCDNGKGFPREMRHRATEPYVT---TRPKGTGLG 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2575951464 649 MPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16944    77 LAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
577-678 3.77e-11

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: 60.52  E-value: 3.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 577 LLNLLTNAVKYtpCGGCVRFETTVAKGAAmgyrqvKFTVSDNGIGMSEEFKEHIFEPFSMEGRSREQGT---GLGMPIVK 653
Cdd:cd16939     5 LDNLLRNALRY--AHRTVRIALLVSGGRL------TLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATggfGLGLAIVH 76
                          90       100
                  ....*....|....*....|....*
gi 2575951464 654 NIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16939    77 RVALWHGGHVECDDSELGGACFRLT 101
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
752-870 5.75e-11

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: 60.51  E-value: 5.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGL-VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIReldreDADA 830
Cdd:cd19932     1 VRVLIAEDEALIRMDLREMLEEAGYeVVGEASDGEEAVELAKKHKP---DLVIMDVKMPRLDGIEAAKIIT-----SENI 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd19932    73 APIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
569-675 6.78e-11

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: 59.78  E-value: 6.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 569 DARRIKQLLLNLLTNAVKYTPCGGCVRFETTVakgaamGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGR--SREQGTG 646
Cdd:cd16945     1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEA------DTEGIELLVFDEGSGIPDYALNRVFERFYSLPRphSGQKSTG 74
                          90       100
                  ....*....|....*....|....*....
gi 2575951464 647 LGMPIVKNIVTMMAGDIAVESTKGQGTTF 675
Cdd:cd16945    75 LGLAFVQEVAQLHGGRITLRNRPDGVLAF 103
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
754-861 7.24e-11

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: 59.83  E-value: 7.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRElDREDADaVPI 833
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP---PDLILLDVMMPGMDGFEVCRRLKA-DPATRH-IPV 75
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPI 861
Cdd:cd19920    76 IFLTALTDTEDKVKGFELGAVDYITKPF 103
glnL PRK11073
nitrogen regulation protein NR(II);
417-682 7.77e-11

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 64.72  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 417 LTFEDKPQLLVVMRDVTADKEIQLSMKDamdVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQL-ARSNPDdrEKVAETL 495
Cdd:PRK11073   94 LTAQRLPEGMILLEMAPMDNQRRLSQEQ---LQHAQQVAARDLVRGLAHEIKNPLGGLRGAAQLlSKALPD--PALTEYT 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 496 KKIGDASDHLLGLINDVLDISKieNGKMTLASepfrlsavLSHVASAVRVQCEQRAQEFVVTT----PPCADavFVGDAR 571
Cdd:PRK11073  169 KVIIEQADRLRNLVDRLLGPQR--PGTHVTES--------IHKVAERVVQLVSLELPDNVRLIrdydPSLPE--LAHDPD 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 572 RIKQLLLNLLTNAVK-YTPCGGCVRFET-TVAKGAAMG--YRQV-KFTVSDNGIGMSEEFKEHIFEPFSmegRSREQGTG 646
Cdd:PRK11073  237 QIEQVLLNIVRNALQaLGPEGGTITLRTrTAFQLTLHGerYRLAaRIDIEDNGPGIPPHLQDTLFYPMV---SGREGGTG 313
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2575951464 647 LGMPIVKNIVTMMAGDIAVESTKGQgTTFTVTFNLR 682
Cdd:PRK11073  314 LGLSIARNLIDQHSGKIEFTSWPGH-TEFSVYLPIR 348
envZ PRK09467
osmolarity sensor protein; Provisional
464-665 9.21e-11

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 64.93  E-value: 9.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 464 SHEIRTPMNVIlgtlQLARS--NPDDrekvaETLKKigdasdhllGLINDVLD--------ISKIENGKmTLASEPFRLS 533
Cdd:PRK09467  237 SHDLRTPLTRI----RLATEmmSEED-----GYLAE---------SINKDIEEcnaiieqfIDYLRTGQ-EMPMEMADLN 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 534 AVLSHVASAVrvqcEQRAQEFVVTTPPCADAVFvGDARRIKQLLLNLLTNAVKYTpcGGCVRFETTVAKgaamgyRQVKF 613
Cdd:PRK09467  298 ALLGEVIAAE----SGYEREIETALQPGPIEVP-MNPIAIKRALANLVVNAARYG--NGWIKVSSGTEG------KRAWF 364
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEPFSM--EGRSREqGTGLGMPIVKNIVTMMAGDIAV 665
Cdd:PRK09467  365 QVEDDGPGIPPEQLKHLFQPFTRgdSARGSS-GTGLGLAIVKRIVDQHNGKVEL 417
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
579-678 2.92e-10

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: 58.07  E-value: 2.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 579 NLLTNAVKYTPCGGCVRFETTVAKGAaMGyRQVKFTVSDNGIGMSEEFKEHIFEP-FSMEGRSREqgtGLGMPIVKNIVT 657
Cdd:cd16915     7 NLIDNALDALAATGAPNKQVEVFLRD-EG-DDLVIEVRDTGPGIAPELRDKVFERgVSTKGQGER---GIGLALVRQSVE 81
                          90       100
                  ....*....|....*....|.
gi 2575951464 658 MMAGDIAVESTKGQGTTFTVT 678
Cdd:cd16915    82 RLGGSITVESEPGGGTTFSIR 102
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
459-656 5.24e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 62.29  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 459 FLSRMSHEIRTPMNVILGTLQL-ARSNPDDrekVAETLKKIgdasDHLLGLINDVLDISKIENgkmTLAS---EPFRL-S 533
Cdd:PRK10755  140 FTADVAHELRTPLAGIRLHLELlEKQHHID---VAPLIARL----DQMMHTVEQLLQLARAGQ---SFSSghyQTVKLlE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 534 AVLSHVASAVRVQCEQRAQEFVVTTPPcADAVFVGDARRIKQLLLNLLTNAVKYTPCGGCVRFETTVAKGAAMgyrqvkF 613
Cdd:PRK10755  210 DVILPSQDELSEMLEQRQQTLLLPESA-ADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIKLSQEDGGAV------L 282
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEPF-SMEgrSREQGTGLGMPIVKNIV 656
Cdd:PRK10755  283 AVEDEGPGIDESKCGELSKAFvRMD--SRYGGIGLGLSIVSRIT 324
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
754-874 6.35e-10

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: 57.25  E-value: 6.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKiGYFDAVLMDVQMPNMNGYEATRCIRELDRedadaVPI 833
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENK-DEFDLVITDVHMPDMDGFEFLELIRLEMD-----LPV 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMrRVLATLIKYV 874
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSI-EDLKNIWQHV 114
PRK11517 PRK11517
DNA-binding response regulator HprR;
752-876 6.95e-10

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 59.91  E-value: 6.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvMFEASKIGYfDAVLMDVQMPNMNGYEATRCIREldredADAV 831
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDG--LYLALKDDY-ALIILDIMLPGMDGWQILQTLRT-----AKQT 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:PRK11517   73 PVICLTARDSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQLRQ 117
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-672 7.46e-10

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: 56.69  E-value: 7.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAVKYTpcGGCVRFETTVAKgaamgyRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE-QGTGLGMPI 651
Cdd:cd16950     1 LKRVLSNLVDNALRYG--GGWVEVSSDGEG------NRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGtSGTGLGLAI 72
                          90       100
                  ....*....|....*....|.
gi 2575951464 652 VKNIVTMMAGDIAVESTKGQG 672
Cdd:cd16950    73 VQRISDAHGGSLTLANRAGGG 93
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
752-860 9.05e-10

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: 56.96  E-value: 9.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAG-LVVERAGDGAEACVMFEAskiGYFDAVLMDVQMPNMNGYEATRCIREldREDADA 830
Cdd:cd19923     1 MKVLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKA---GGFDFVITDWNMPNMDGLELLKTIRA--DGALSH 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd19923    76 LPVLMVTAEAKKENVIAAAQAGVNNYIVKP 105
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
754-860 1.15e-09

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: 56.29  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMfeASKIGYfDAVLMDVQMPNMNGYEAtrcIRELdREDADAVPI 833
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHL--ALTNEY-DLIILDVMLPGLDGLEV---LRRL-RAAGKQTPV 73
                          90       100
                  ....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd19935    74 LMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
754-876 1.32e-09

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: 56.52  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDN-DLNAEIAcELLAEAGLVVERAGDGAEAcvMFEASKIGYfDAVLMDVQMPNMNGYEATRCIRELDRedadAVP 832
Cdd:cd19934     1 LLLVEDDaLLAAQLK-EQLSDAGYVVDVAEDGEEA--LFQGEEEPY-DLVVLDLGLPGMDGLSVLRRWRSEGR----ATP 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:cd19934    73 VLILTARDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALIRR 116
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
752-809 1.44e-09

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: 54.50  E-value: 1.44e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2575951464  752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMP 809
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK---PDLILLDIMMP 55
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
753-864 1.77e-09

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: 56.06  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEAtrcIRELDREDADaVP 832
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ---PDLVLCDLRMPEMDGLEV---LKQITKESPD-TP 74
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPI-DMR 864
Cdd:cd17555    75 VIVVSGAGVMSDAVEALRLGAWDYLTKPIeDLA 107
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
753-860 2.69e-09

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: 55.20  E-value: 2.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASkiGYFDAVLMDVQMPNMNGYEATRCIRELDredaDAVP 832
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQG--KDIDIVVTDIVMPEMDGIELAREARKID----PDVK 74
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd18160    75 ILFISGGAAAAPELLSDAVGDNATLKKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
754-877 3.11e-09

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: 55.39  E-value: 3.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIREldredADAVPI 833
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQG---LAALLEGSPDLVVLDVMLPKMNGLDVLKELRK-----TSQVPV 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATlIKYVRKR 877
Cdd:cd17623    73 LMLTARGDDIDRILGLELGADDYLPKPFNPRELVAR-IRAILRR 115
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
562-679 6.69e-09

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: 54.95  E-value: 6.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 562 ADAVFVGDARRIKQLLLNLLTNAVKYtpcggCVRF-ETTVAKGAAmgyrQVKFTVSDNGIGMSEEFKEHIFEPfSMEGRS 640
Cdd:cd16954    27 PELRFPGERNDLMELLGNLLDNACKW-----CLEFvEVTARQTDG----GLHLIVDDDGPGVPESQRSKIFQR-GQRLDE 96
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2575951464 641 REQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16954    97 QRPGQGLGLAIAKEIVEQYGGELSLSDSPLGGARFEVVF 135
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
753-842 6.77e-09

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: 54.71  E-value: 6.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGL--VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRE-------- 822
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDPDieVVGTARDGEEALEKIKELKP---DVITLDIEMPVMDGLEALRRIMAerptpvvm 78
                          90       100
                  ....*....|....*....|...
gi 2575951464 823 ---LDREDADAVpIIAMSANAFA 842
Cdd:cd17541    79 vssLTEEGAEIT-LEALELGAVD 100
PRK10610 PRK10610
chemotaxis protein CheY;
752-879 6.86e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 54.98  E-value: 6.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGL-VVERAGDGAEACVMFEAskiGYFDAVLMDVQMPNMNGYEATRCIRElDREDAdA 830
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQA---GGFGFVISDWNMPNMDGLELLKTIRA-DGAMS-A 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPIdmrrVLATLIKYVRKRYE 879
Cdd:PRK10610   81 LPVLMVTAEAKKENIIAAAQAGASGYVVKPF----TAATLEEKLNKIFE 125
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
752-876 9.25e-09

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.86  E-value: 9.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDRedadAV 831
Cdd:PRK09836    1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNG---YHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANK----GM 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:PRK09836   74 PILLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
574-682 1.05e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 58.49  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 574 KQLLLNLLTNAVKY----TPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRsreqGTGLGM 649
Cdd:COG2972   338 KLILQPLVENAIEHgiepKEGGGTIRISIRKEGD------RLVITVEDNGVGMPEEKLEKLLEELSSKGE----GRGIGL 407
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 650 PIVKNIVTMMAGD---IAVESTKGQGTTFTVTFNLR 682
Cdd:COG2972   408 RNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLE 443
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
771-876 1.20e-08

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: 53.93  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdadaVPIIAMSANAFAEDVSASLA 850
Cdd:cd17627    18 LRFEGYEVETAVDGAEALRVISGNRP---DAVVLDVMMPRLDGLEVCRRLRAAGND----LPILVLTARDSVSDRVAGLD 90
                          90       100
                  ....*....|....*....|....*.
gi 2575951464 851 SGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:cd17627    91 AGADDYLVKPFALEELLARVRALLRR 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
752-824 1.34e-08

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: 54.13  E-value: 1.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2575951464 752 LRVLLAEDNDLNAE-IACELLAEAGL-VVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCI---RELD 824
Cdd:COG2197     2 IRVLIVDDHPLVREgLRALLEAEPDIeVVGEAADGEEALELLEELR---PDVVLLDIRMPGMDGLEALRRLltpRERE 76
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
753-868 1.84e-08

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: 53.24  E-value: 1.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldredADAVP 832
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRP---DLVLLDLMLPGIDGIEVCRQIRA-----ESGVP 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17626    74 IVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELVA 109
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
273-682 2.12e-08

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 57.61  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 273 VRAEAAVVTTTFEAVFAIIFACLVVVALLVFGAYRRRLREQNVAMLGQLYEALSDSIDMAVNLYSPTDGKVTPIVAKAER 352
Cdd:COG3920   118 LLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAA 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 353 IIGYRLDAFLQNERLAATIGLSPEGVALFDRIRKDETKGFEQGEFSFRSKQTGKECWASYSVKRLTFEDKPQLLVVMRDV 432
Cdd:COG3920   198 ALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLV 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 433 TADkeiqlsMKDAMDVAEAANAAKsEFLSR-MSHEIRTPMNVILGTLQLARSNPDDrEKVAETLKkigDASDHL--LGLI 509
Cdd:COG3920   278 ITE------RKRAEEELEASLEEK-ELLLReLHHRVKNNLQVVSSLLRLQARRADD-PEAREALE---ESQNRIqaLALV 346
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 510 NDVL----DISKIEngkmtlasepfrLSAVLSHVASAVRVQCEQRAQEFVVTTPPCA----DAVFVGdarrikqLLLN-L 580
Cdd:COG3920   347 HELLyqseDWEGVD------------LRDYLRELLEPLRDSYGGRGIRIELDGPDVElpadAAVPLG-------LILNeL 407
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 581 LTNAVKY---TPCGGCVRFETTVAKGaamgyrQVKFTVSDNGIGMSEEFkehifepfsmegrSREQGTGLGMPIVKNIVT 657
Cdd:COG3920   408 VTNALKHaflSGEGGRIRVSWRREDG------RLRLTVSDNGVGLPEDV-------------DPPARKGLGLRLIRALVR 468
                         410       420
                  ....*....|....*....|....*
gi 2575951464 658 MMAGDIAVEStkGQGTTFTVTFNLR 682
Cdd:COG3920   469 QLGGTLELDR--PEGTRVRITFPLA 491
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
426-678 2.20e-08

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 58.02  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 426 LVVMRDvtADKEIQLS--MKDAMDVAEAANAAKSEFLSRMSHEIRTPMNVILGTLQLARsNPDDREKVAETLKKIGDASD 503
Cdd:PRK10618  420 LFLLRD--QDREVLVNkkLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLR-QTSDEEQQQPELDQLAEQSD 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 504 HLLGLINDVLDISKIENGKMTLASEPFRLSAVLSHVASAVRVQCEQRAQEFVVTTPPCADAVFVGDARRIKQLLLNLLTN 583
Cdd:PRK10618  497 VLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNY 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 584 AVKYTPCGGcVRFETTVAKGAAmgyRQVKFTVSDNGIGMSEEFKEHIFEPF---SMEGRSReQGTGLGMPIVKNIVTMMA 660
Cdd:PRK10618  577 AITTTAYGK-ITLEVDQDESSP---DRLTIRILDTGAGVSIKELDNLHFPFlnqTQGDRYG-KASGLTFFLCNQLCRKLG 651
                         250
                  ....*....|....*...
gi 2575951464 661 GDIAVESTKGQGTTFTVT 678
Cdd:PRK10618  652 GHLTIKSREGLGTRYSIH 669
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
753-870 2.24e-08

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: 53.15  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGL--VVERAGDGAEACVMFEASkigyfDAVLMDVQMPNMNGYEATRCIReldreDADA 830
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFnvVVEHRGDRALEVIAREKP-----DAVLLDIMLPGIDGLTLCRDLR-----PKYQ 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17622    72 GPILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARL 111
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
771-876 3.31e-08

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: 52.69  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDRedADAVPIIAMSANAFAEDVSASLA 850
Cdd:cd17562    20 LRGAGYEVVEAADGRDALSKAQSKK---FDLIITDQNMPNMDGIELIKELRKLPA--YKFTPILMLTTESSDEKKQEGKA 94
                          90       100
                  ....*....|....*....|....*.
gi 2575951464 851 SGMNAHLSKPIDMRRvlatLIKYVRK 876
Cdd:cd17562    95 AGATGWLVKPFDPEQ----LLEVVKK 116
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
754-868 5.40e-08

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: 52.03  E-value: 5.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIReLDREDadaVPI 833
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEG---LDLGKLYDYDIILLDLNLPDMSGYEVLRTLR-LAKVK---TPI 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17616    74 LILSGLADIEDKVKGLGFGADDYMTKPFHKDELVA 108
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
753-876 5.50e-08

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: 51.97  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIreldREDADAVP 832
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRP---DAVVLDIMLPDMDGLEVLRRL----RADGPDVP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:cd17615    74 VLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALLRR 117
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
614-689 6.32e-08

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 56.07  E-value: 6.32e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2575951464 614 TVSDNGIGMSEEFKEHIFEP-FSMEGRSReqgtGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVtfnlRIALEAER 689
Cdd:PRK11086  471 EVSDDGPGIAPDEIDAIFDKgYSTKGSNR----GVGLYLVKQSVENLGGSIAVESEPGVGTQFFV----QIPWDGER 539
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
754-838 6.87e-08

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: 51.57  E-value: 6.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNdlnaEIACELLA------EAGL-VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRE 826
Cdd:cd17536     1 VLIVDDE----PLIREGLKklidweELGFeVVGEAENGEEALELIEEHKP---DIVITDIRMPGMDGLELIEKIRELYPD 73
                          90
                  ....*....|..
gi 2575951464 827 dadaVPIIAMSA 838
Cdd:cd17536    74 ----IKIIILSG 81
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
754-876 1.00e-07

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: 51.27  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldredADAVPI 833
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQP---DLILLDLMLPEKDGLEVCREVRK-----TSNVPI 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:cd17614    73 IMLTAKDSEVDKVLGLELGADDYVTKPFSNRELLARVKANLRR 115
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
754-860 1.98e-07

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: 50.07  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIGY------FDAVLMDVQMPNMNGYEATRCIRElDRED 827
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGndlskeLDLIITDIEMPKMDGYELTFELRD-DPRL 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2575951464 828 ADaVPIIAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd19924    80 AN-IPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
750-872 2.16e-07

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 54.27  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDredaD 829
Cdd:PRK10365    4 DNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQA---LEQVREQVFDLVLCDVRMAEMDGIATLKEIKALN----P 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2575951464 830 AVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIK 872
Cdd:PRK10365   77 AIPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
573-677 2.18e-07

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: 49.76  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 573 IKQLLLNLLTNAvkYTPCGGCVRFETTVAKGAAMGyrQVKFTVSDNGIGMSEEFKEHIFEPFsMEGRSREQGTGLGMPIV 652
Cdd:cd16976     1 IQQVLMNLLQNA--LDAMGKVENPRIRIAARRLGG--RLVLVVRDNGPGIAEEHLSRVFDPF-FTTKPVGKGTGLGLSIS 75
                          90       100
                  ....*....|....*....|....*
gi 2575951464 653 KNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:cd16976    76 YGIVEEHGGRLSVANEEGAGARFTF 100
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
753-870 3.07e-07

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: 51.46  E-value: 3.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEatrCIRELDREDADAvP 832
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEA---LALLEQAPPDYAVLDLRLGDGSGLD---LIEALRERDPDA-R 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2575951464 833 IIAMSanAFAEDVSASLASGMNAH--LSKPIDMRRVLATL 870
Cdd:COG4567    79 IVVLT--GYASIATAVEAIKLGADdyLAKPADADDLLAAL 116
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
753-868 3.27e-07

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: 49.68  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldredADAVP 832
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQP---SLVVLDIMLPGMDGLTVCREVRE-----HSHVP 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd19939    73 ILMLTARTEEMDRVLGLEMGADDYLCKPFSPRELLA 108
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
752-873 5.35e-07

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: 49.17  E-value: 5.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAG--LVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDREdad 829
Cdd:cd19925     1 INVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQP---DLILLDIYLPDGNGLDLLRELRAAGHD--- 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 830 aVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKY 873
Cdd:cd19925    75 -VDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
568-681 1.33e-06

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: 48.04  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 568 GDARRIKQLLLNLLTNAVKYTP-CGGCVRFETTVAK---GAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPfsMEGRSREq 643
Cdd:cd16932     2 GDQIRLQQVLADFLLNAVRFTPsPGGWVEIKVSPTKkqiGDGVHVIHLEFRITHPGQGLPEELVQEMFEE--NQWTTQE- 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2575951464 644 gtGLGMPIVKNIVTMMAGDiaVESTKGQGT-TFTVTFNL 681
Cdd:cd16932    79 --GLGLSISRKLVKLMNGD--VRYLREAGRsYFLITLEL 113
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
754-870 1.79e-06

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: 47.66  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAED-NDLNAEIAcELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRedadaVP 832
Cdd:cd18159     1 ILIVEDdETIASLLK-KHLEKWGYEVVLIEDFEDVLEEFLQFKP---DLVLLDINLPYFDGFYWCREIRQISN-----VP 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd18159    72 IIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
753-878 1.94e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 49.80  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASkigyFDAVLMDVQMPNMNGYEATRCIRELDRedadaVP 832
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS----IDLLLLDVMMPKKNGIDTLKELRQTHQ-----TP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRKRY 878
Cdd:PRK10955   74 VIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRSH 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
769-870 2.56e-06

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: 47.11  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 769 ELLAEAGLVVERAGDGAEACVMFEASkigYFDAVLMDVQMPNMNGYEATRCIRELDREdadaVPIIAMSANAFAEDVSAS 848
Cdd:cd17550    16 GILEDEGYEVDTAADGEEALKLIKER---RPDLVLLDIWLPDMDGLELLKEIKEKYPD----LPVIMISGHGTIETAVKA 88
                          90       100
                  ....*....|....*....|..
gi 2575951464 849 LASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17550    89 TKLGAYDFIEKPLSLDRLLLTI 110
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
579-678 3.23e-06

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: 46.61  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 579 NLLTNAVKYTPCggcvrfETTVAKGAAMGYRQVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE-QGTGLGMPIVKNIVT 657
Cdd:cd16923     7 NLLSNAIKYSPE------NTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNtEGAGLGLSIAKAIIE 80
                          90       100
                  ....*....|....*....|.
gi 2575951464 658 MMAGDIAVEStKGQGTTFTVT 678
Cdd:cd16923    81 LHGGSASAEY-DDNHDLFKVR 100
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
754-860 3.55e-06

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: 46.22  E-value: 3.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDreDADAVPI 833
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEA---LDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNA--DFDTIPV 75
                          90       100
                  ....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd19927    76 IFLTAKGMTSDRIKGYNAGCDGYLSKP 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
480-682 4.17e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 49.23  E-value: 4.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 480 LARSNPDDREKVAETLKKIGDASDHLLGLINDVL-DISKIENGKMTLASEpfrLSAVLSHVASAVRVQCEQRAQEFVVTT 558
Cdd:COG4585    79 ARRLLDADPEAAREELEEIRELAREALAELRRLVrGLRPPALDDLGLAAA---LEELAERLLRAAGIRVELDVDGDPDRL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 559 PP-CADAVFvgdarRIKQlllNLLTNAVKYtpcGGCVRFETTVAKGAamgyRQVKFTVSDNGIGMSEEfkehifepfsme 637
Cdd:COG4585   156 PPeVELALY-----RIVQ---EALTNALKH---AGATRVTVTLEVDD----GELTLTVRDDGVGFDPE------------ 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2575951464 638 grsREQGTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTFNLR 682
Cdd:COG4585   209 ---AAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
753-868 5.35e-06

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: 46.09  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDgAEACVMFEASKigYFDAVLMDVQMPNMNGYEATRCIREldREDADAVP 832
Cdd:cd17618     2 TILIVEDEPAIREMIAFNLERAGFDVVEAED-AESAVNLIVEP--RPDLILLDWMLPGGSGIQFIRRLKR--DEMTRDIP 76
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17618    77 IIMLTARGEEEDKVRGLEAGADDYITKPFSPRELVA 112
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
436-668 5.44e-06

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 50.07  E-value: 5.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 436 KEIQLSMKDAMD--VAEAANAAKSEFLSRMSHEIRTPMNVI---LGTLQLARSNPDDrEKVAETLKKIGDASDHLLGLIN 510
Cdd:COG4192   411 KRIEKNLRQTQDelIQAAKMAVVGQTMTSLAHELNQPLNAMsmyLFSAKKALEQENY-AQLPTSLDKIEGLIERMDKIIK 489
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 511 DVLDISKIENGKMTLASepfrlsaVLSHVASA-VRVQCEQRAQEFVVTTPPcaDAVFVGDARRIKQLLLNLLTNAVKYTP 589
Cdd:COG4192   490 SLRQFSRKSDTPLQPVD-------LRQVIEQAwELVESRAKPQQITLHIPD--DLMVQGDQVLLEQVLVNLLVNALDAVA 560
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 590 CGGCVrfetTVAKGAAMGYRQVkfTVSDNGIGMseEFKEHIFEPFSMegrSREQGTGLGMPIVKNIVTMMAGDIAVEST 668
Cdd:COG4192   561 TQPQI----SVDLLSNAENLRV--AISDNGNGW--PLVDKLFTPFTT---TKEVGLGLGLSICRSIMQQFGGDLYLAST 628
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
460-679 5.62e-06

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 50.02  E-value: 5.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 460 LSRMSHEIRTPMNVILGTLQLARSNPDDREKVAE--TLKKIGDASDHllglINDVLDISKIENGKMTLASEPFRLSAVLS 537
Cdd:PRK10815  270 LTDLTHSLKTPLAVLQSTLRSLRSGKQMSVEQAEpiMLEQISRISQQ----IGYYLHRASMRSEHNLLSRELHSVAPLLD 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 538 HVASAVRvQCEQRaQEFVVTTPPCADAVFVGDARRIKQLLLNLLTNAVKYtpcggCVRFettVAKGAAMGYRQVKFTVSD 617
Cdd:PRK10815  346 NLTSALN-KVYQR-KGVNITLDISPEITFVGEKNDFMEVMGNVLDNACKY-----CLEF---VEISARQTDEHLHIVVED 415
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2575951464 618 NGIGMSEEFKEHIFEpfsmegrsREQ-------GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVTF 679
Cdd:PRK10815  416 DGPGIPESKRELIFD--------RGQradtlrpGQGLGLSVAREITEQYEGKISAGDSPLGGARMEVIF 476
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
754-868 5.75e-06

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: 45.90  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAE-ACVMFEASkigyFDAVLMDVQMPNMNGYEATRCIREldredADAVP 832
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEeARLMLHRR----VDLVLLDLRLGQESGLDLLRTIRA-----RSDVP 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2575951464 833 IIAMSANAFAE-DVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd17594    73 IIIISGDRRDEiDRVVGLELGADDYLAKPFGLRELLA 109
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
754-870 6.16e-06

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: 46.04  E-value: 6.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIreldREDADAVPI 833
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP---PDVVLLDLKLPDMSGMEILKWI----QERSLPTSV 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2575951464 834 IAMSANAFAEdvSASLASGMNAH--LSKPIDMRRVLATL 870
Cdd:cd17572    74 IVITAHGSVD--IAVEAMRLGAYdfLEKPFDADRLRVTV 110
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
630-677 7.68e-06

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: 47.19  E-value: 7.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 630 IFEP-FSMegrsREQ-----GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTV 677
Cdd:cd16916   126 IFAPgFST----AEQvtdvsGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTI 175
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
753-860 8.88e-06

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: 45.59  E-value: 8.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigYFDAVLMDVQMPNMNGYEATRCIREldREDADAVP 832
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHP--DIKLVITDYNMPEMDGFELVREIRK--KYSRDQLA 77
                          90       100
                  ....*....|....*....|....*....
gi 2575951464 833 IIAMSANAfAEDVSAS-LASGMNAHLSKP 860
Cdd:cd17544    78 IIGISASG-DNALSARfIKAGANDFLTKP 105
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
771-860 1.31e-05

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: 44.46  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRELDredadAVPIIAMSANAFAEDVSASLA 850
Cdd:cd17620    18 LEAHGYRVFEAETGQEGLLEAATRK---PDLIILDLGLPDMDGLEVIRRLREWS-----AVPVIVLSARDEESDKIAALD 89
                          90
                  ....*....|
gi 2575951464 851 SGMNAHLSKP 860
Cdd:cd17620    90 AGADDYLTKP 99
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
753-867 1.41e-05

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: 45.07  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRedadaVP 832
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI---DLVLLDINLPGKDGLSLTRELREQSE-----VG 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVL 867
Cdd:cd17619    74 IILVTGRDDEVDRIVGLEIGADDYVTKPFNPRELL 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
753-862 1.79e-05

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: 44.85  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLA-EAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYeATrcIRELDREDA-DA 830
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQP---DAILLDVMMPDMDGL-AT--LKKLQANPEtQS 76
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPID 862
Cdd:cd17552    77 IPVILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
630-678 1.86e-05

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 48.25  E-value: 1.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2575951464 630 IFEP-FSmegrSREQ-----GTGLGMPIVKNIVTMMAGDIAVESTKGQGTTFTVT 678
Cdd:COG0643   365 IFAPgFS----TAEEvtdlsGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLR 415
PRK15479 PRK15479
transcriptional regulator TctD;
752-876 2.04e-05

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 46.64  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDG--AEACVMFEAskigyFDAVLMDVQMPNMNGYEATRCIreldREDAD 829
Cdd:PRK15479    1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGlaADHLLQSEM-----YALAVLDINMPGMDGLEVLQRL----RKRGQ 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2575951464 830 AVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:PRK15479   72 TLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRR 118
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
754-860 2.89e-05

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: 43.73  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldredADAVPI 833
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGA---DIVLLDLMLPGLSGTEVCRQLRA-----RSNVPV 72
                          90       100
                  ....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd17621    73 IMVTAKDSEIDKVVGLELGADDYVTKP 99
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
754-878 3.22e-05

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: 44.23  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAE-IACELLAEAGLVVEraGDGAEAcvMFEASKiGYFDAVLMDVQMPNMNGYEATRCIRELDRedADAVP 832
Cdd:cd17539     1 VLLVDDRPSSAErIAAMLSSEHEVVVE--ADPDEA--LFRAAE-GPFDLVIVSLALEDFDGLRLCSQLRSLER--TRQLP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYVR-KRY 878
Cdd:cd17539    74 ILAVADPGDRGRLIRALEIGVNDYLVRPIDPNELLARVRTQIRrKRY 120
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
754-860 3.24e-05

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 43.54  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEAsKIGYFDAVLMDVQMPNMNGYEATRCIREldREDADAVPI 833
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLED-EQNEIDLILTEVDLPVSSGFKLLSYIMR--HKICKNIPV 77
                          90       100
                  ....*....|....*....|....*..
gi 2575951464 834 IAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
754-860 4.74e-05

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: 43.10  E-value: 4.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIgyFDAVLMDVQMPN-MNGYEATRCIRELDREdadaVP 832
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPD--IDLLVTDVIMPGgMNGSQLAEEARRRRPD----LK 74
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAhLSKP 860
Cdd:cd18161    75 VLLTSGYAENAIEGGDLAPGVDV-LSKP 101
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
753-868 6.38e-05

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: 43.14  E-value: 6.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIReldreDADAVP 832
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQV---LPYVRHTPPDLILLDLMLPGTDGLTLCREIR-----RFSDVP 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2575951464 833 IIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLA 868
Cdd:cd19938    73 IIMVTARVEEIDRLLGLELGADDYICKPYSPREVVA 108
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
752-873 7.30e-05

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: 43.20  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAG-LVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldREDADA 830
Cdd:cd17530     1 LRVLVLDDDPFQCMMAATILEDLGpGNVDEADDGREALVILLCNAP---DIIICDLKMPDMDGIEFLRHLAE--SHSNAA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2575951464 831 VPII-AMSANAFAEDVSASLASGMN--AHLSKPIDMRRVLATLIKY 873
Cdd:cd17530    76 VILMsGLDGGILESAETLAGANGLNllGTLSKPFSPEELTELLTKY 121
PRK10336 PRK10336
two-component system response regulator QseB;
752-876 8.23e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.89  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 752 LRVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACvmfEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREDadav 831
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGK---EALYSAPYDAVILDLTLPGMDGRDILREWREKGQRE---- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2575951464 832 PIIAMSA-NAFAEDVSAsLASGMNAHLSKPIDMRRVLATLIKYVRK 876
Cdd:PRK10336   74 PVLILTArDALAERVEG-LRLGADDYLCKPFALIEVAARLEALMRR 118
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
754-877 1.70e-04

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: 42.09  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKIGyfdAVLMDVQMPNMNGYEATRCIRELDREdadaVPI 833
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPG---VVISDIRMPGMDGLELLAQIRELDPD----LPV 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2575951464 834 IAMSANAfaeDVS-ASLASGMNAH--LSKPIDMRRVLATLIKYVRKR 877
Cdd:cd17549    74 ILITGHG---DVPmAVEAMRAGAYdfLEKPFDPERLLDVVRRALEKR 117
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
530-681 1.71e-04

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 42.21  E-value: 1.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 530 FRLSAVLSHVAsAVRVQCEQRAQEFVVTTPPCADAVfvgdarrikqLLLN-LLTNAVKYTPCG---GCVRFETTVAKGaa 605
Cdd:COG2172     2 LSLPADLEDLG-LARRAVRALLRELGLDEDDADDLV----------LAVSeAVTNAVRHAYGGdpdGPVEVELELDPD-- 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2575951464 606 mgyrQVKFTVSDNGIGMSEEfkeHIFEPFSMEGRSreqgtGLGMPIVKNIVTmmagDIAVESTKGqGTTFTVTFNL 681
Cdd:COG2172    69 ----GLEIEVRDEGPGFDPE---DLPDPYSTLAEG-----GRGLFLIRRLMD----EVEYESDPG-GTTVRLVKRL 127
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
800-860 1.81e-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: 41.59  E-value: 1.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 800 DAVLMDVQMPNMNGYEATRCIRELdrEDADAVPIIAMSAN-AFAEDVSASLAsGMNAHLSKP 860
Cdd:cd17602    44 DLILIDIDMPDLDGYELCSLLRKS--SALKDTPIIMLTGKdGLVDRIRAKMA-GASGYLTKP 102
pleD PRK09581
response regulator PleD; Reviewed
753-862 2.46e-04

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 44.51  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEiacelLAEAGLVVE-----RAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRElDRED 827
Cdd:PRK09581    4 RILVVDDIPANVK-----LLEAKLLAEyytvlTASSGAEAIAICEREQP---DIILLDVMMPGMDGFEVCRRLKS-DPAT 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2575951464 828 ADaVPIIAMSANAFAEDVSASLASGMNAHLSKPID 862
Cdd:PRK09581   75 TH-IPVVMVTALDDPEDRVRGLEAGADDFLTKPIN 108
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
575-666 2.60e-04

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: 41.40  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 575 QLLLNLLTNAVKYTPcGGCVRFETTVAKGAAMgyrqVKFTVSDNGIGMSEEFKEHIFEPFSMEGRSRE---QGTGLGMPI 651
Cdd:cd16953     3 QVLRNLIGNAISFSP-PDTGRITVSAMPTGKM----VTISVEDEGPGIPQEKLESIFDRFYTERPANEafgQHSGLGLSI 77
                          90
                  ....*....|....*
gi 2575951464 652 VKNIVTMMAGDIAVE 666
Cdd:cd16953    78 SRQIIEAHGGISVAE 92
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
771-870 2.87e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 43.09  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldrEDADAvPIIAMSANAFAEDVSASLA 850
Cdd:PRK10651   28 MAPDITVVGEASNGEQGIELAESLDP---DLILLDLNMPGMNGLETLDKLRE---KSLSG-RIVVFSVSNHEEDVVTALK 100
                          90       100
                  ....*....|....*....|
gi 2575951464 851 SGMNAHLSKPIDMRRVLATL 870
Cdd:PRK10651  101 RGADGYLLKDMEPEDLLKAL 120
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
771-872 3.15e-04

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: 41.10  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIreldREDADAVPIIAMSANAFAEDVSASLA 850
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASSQP---DVLISDIRMPGMDGLALLAQI----KQRHPDLPVIIMTAHSDLDSAVSAYQ 92
                          90       100
                  ....*....|....*....|..
gi 2575951464 851 SGMNAHLSKPIDMRRVLAtLIK 872
Cdd:cd19919    93 GGAFEYLPKPFDIDEAVA-LVE 113
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
581-679 3.73e-04

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: 40.23  E-value: 3.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 581 LTNAVKYTPCGGC-VRFETTVakgaamgyRQVKFTVSDNGIGmseefkehifepFSMEGRSREQGTGL-GMpivKNIVTM 658
Cdd:cd16917     9 LTNALKHAGASRVrVTLSYTA--------DELTLTVVDDGVG------------FDGPAPPGGGGFGLlGM---RERAEL 65
                          90       100
                  ....*....|....*....|.
gi 2575951464 659 MAGDIAVESTKGQGTTFTVTF 679
Cdd:cd16917    66 LGGTLTIGSRPGGGTRVTARL 86
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
770-873 7.95e-04

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: 39.83  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 770 LLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREdadaVPIIAMSANAFAEDVSASL 849
Cdd:cd17593    20 LPADWDVEITFAENGEEA---LEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLE----TKVIVVSGDVQPEAKERVL 92
                          90       100
                  ....*....|....*....|....
gi 2575951464 850 ASGMNAHLSKPIDMRRVLATLIKY 873
Cdd:cd17593    93 ELGALAFLKKPFDPEKLAQLLEEL 116
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
750-879 9.55e-04

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: 39.83  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 750 EGLRVLLAEDNDLnaeiacELLAEAGlvveragDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDRedad 829
Cdd:cd17532    12 EELRYLLEEHPDI------EIVGEAE-------NGEEALEAIEELKP---DVVFLDIQMPGLDGLELAKKLSKLAK---- 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2575951464 830 aVPIIAMsANAFaeDVSASLASGMNA--HLSKPIDMRRvLATLIKYVRKRYE 879
Cdd:cd17532    72 -PPLIVF-VTAY--DEYAVEAFELNAvdYLLKPFSEER-LAEALAKLRKRLS 118
orf27 CHL00148
Ycf27; Reviewed
771-879 9.71e-04

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 41.63  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 771 LAEAGLVVERAGDGAEACVMFeasKIGYFDAVLMDVQMPNMNGYEATRCIreldREDADaVPIIAMSAnafAEDVS---A 847
Cdd:CHL00148   26 LSIIGYEVITASDGEEALKLF---RKEQPDLVILDVMMPKLDGYGVCQEI----RKESD-VPIIMLTA---LGDVSdriT 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2575951464 848 SLASGMNAHLSKPIDMRRVLATlIKYVRKRYE 879
Cdd:CHL00148   95 GLELGADDYVVKPFSPKELEAR-IRSVLRRTN 125
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
754-822 1.21e-03

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: 39.56  E-value: 1.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 754 VLLAEDNDLNAEIACELL--AEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEATRCIRE 822
Cdd:cd19930     1 VLIAEDQEMVRGALAALLelEDDLEVVAQASNGQEALRLVLKHS---PDVAILDIEMPGRTGLEVAAELRE 68
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
753-877 1.73e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.86  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASkigYFDAVLMDVQMPNMNGYEAtrcIRELDREDADA-V 831
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEP---WPDLILLDWMLPGGSGIQF---IKHLKRESMTRdI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2575951464 832 PIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATlIKYVRKR 877
Cdd:PRK10161   78 PVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVAR-IKAVMRR 122
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
751-874 1.86e-03

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: 39.07  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 751 GLRVLLAEdndlnaeiaceLLAEAGLVVERAGDGAEAcvmFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELDREdada 830
Cdd:cd17553    11 GIRILLNE-----------VFNKEGYQTFQAANGLQA---LDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDEN---- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2575951464 831 VPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATLIKYV 874
Cdd:cd17553    73 IRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
753-870 2.22e-03

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: 38.58  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLAEAGLVVERAGDGAEACVMFEASKigyFDAVLMDVQMPNMNGYEatrCIRELDREDADAVP 832
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEK---PDYAVLDLRLGGDSGLD---LIPPLRALQPDARI 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2575951464 833 IIAMSANAFAEDVSAsLASGMNAHLSKPIDMRRVLATL 870
Cdd:cd17563    76 VVLTGYASIATAVEA-IKLGADDYLAKPADADEILAAL 112
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
800-870 2.85e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.17  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2575951464 800 DAVLMDVQMPNMNGYEATRCIRELDredadAVPIIAMSANAFAEDVSASLASGMNAHLSKPIDMRRVLATL 870
Cdd:PRK10529   47 DLIILDLGLPDGDGIEFIRDLRQWS-----AIPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARL 112
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
770-870 3.69e-03

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: 39.70  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 770 LLAEAGLVVERAGDGAEACVMFEASKIGyfdAVLMDVQMPNMNGYEatrCIRELdREDADAVPIIAMSANAfaeDVSASL 849
Cdd:COG4566    18 LLESAGLRVETFASAEAFLAALDPDRPG---CLLLDVRMPGMSGLE---LQEEL-AARGSPLPVIFLTGHG---DVPMAV 87
                          90       100
                  ....*....|....*....|....*
gi 2575951464 850 ASgMNA----HLSKPIDMRRVLATL 870
Cdd:COG4566    88 RA-MKAgavdFLEKPFDDQALLDAV 111
PRK10693 PRK10693
two-component system response regulator RssB;
781-873 3.91e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 40.36  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 781 AGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIRELDredaDAVPIIAMSANAFAEDVSASLASGMNAHLSKP 860
Cdd:PRK10693    3 AANGVDALELLGGFTP---DLIICDLAMPRMNGIEFVEHLRNRG----DQTPVLVISATENMADIAKALRLGVQDVLLKP 75
                          90
                  ....*....|....
gi 2575951464 861 I-DMRRVLATLIKY 873
Cdd:PRK10693   76 VkDLNRLREMVFAC 89
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
597-685 4.44e-03

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 40.87  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 597 ETTVAKGAAMGyrqvkFTVSDNgigMS-EEFKEHIFEP-FSmegrSREQ-----GTGLGMPIVKNIVTMMAGDIAVESTK 669
Cdd:PRK10547  444 ERILAKAASQG-----LAVSEN---MSdEEVGMLIFAPgFS----TAEQvtdvsGRGVGMDVVKRNIQEMGGHVEIQSKQ 511
                          90
                  ....*....|....*.
gi 2575951464 670 GQGTTFTVTFNLRIAL 685
Cdd:PRK10547  512 GKGTTIRILLPLTLAI 527
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
753-820 4.55e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 40.25  E-value: 4.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 753 RVLLAEDNDLNAEIACELLA-EAGL-VVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCI 820
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALArDPDHeVVWVATDGAQAVERCAAQPP---DVILMDLEMPRMDGVEATRRI 68
PRK13560 PRK13560
hypothetical protein; Provisional
576-679 4.67e-03

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 40.81  E-value: 4.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 576 LLLNLLTNAVKYT-PCGGCVRFETTVAKgaaMGYRQVKFTVSDNGIGMseefkehifePFSMEGRSREQgtgLGMPIVKN 654
Cdd:PRK13560  715 IISELLSNALKHAfPDGAAGNIKVEIRE---QGDGMVNLCVADDGIGL----------PAGFDFRAAET---LGLQLVCA 778
                          90       100
                  ....*....|....*....|....*
gi 2575951464 655 IVTMMAGDIAVESTKgqGTTFTVTF 679
Cdd:PRK13560  779 LVKQLDGEIALDSRG--GARFNIRF 801
PAS COG2202
PAS domain [Signal transduction mechanisms];
307-469 4.94e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 4.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 307 RRRLREQNVAMLGQLYEALSDSIDMAvnlysPTDGKVTPIVAKAERIIGYRLDAFL-QNERLAATIGLSPEGVALFDRIR 385
Cdd:COG2202     2 AEEALEESERRLRALVESSPDAIIIT-----DLDGRILYVNPAFERLTGYSAEELLgKTLRDLLPPEDDDEFLELLRAAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 386 KDEtkGFEQGEFSFRSKQtGKECWASYSVKRLTFED--KPQLLVVMRDVTADKEIQLSMKDAMDVAEAANAAKSEFLSRM 463
Cdd:COG2202    77 AGG--GVWRGELRNRRKD-GSLFWVELSISPVRDEDgeITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153

                  ....*.
gi 2575951464 464 SHEIRT 469
Cdd:COG2202   154 DLDGRI 159
PAS COG2202
PAS domain [Signal transduction mechanisms];
308-439 4.99e-03

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 308 RRLREQNvamlgQLYEALSDSIDMAVNLYSPtDGKVTPIVAKAERIIGYRLDAFLQneRLAATIGLSPEGVALFDRIRKD 387
Cdd:COG2202   130 EALRESE-----ERLRLLVENAPDGIFVLDL-DGRILYVNPAAEELLGYSPEELLG--KSLLDLLHPEDRERLLELLRRL 201
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2575951464 388 ETKGFEQGEFSFRSK-QTGKECWASYSVKRLTFEDKPQ-LLVVMRDVTADKEIQ 439
Cdd:COG2202   202 LEGGRESYELELRLKdGDGRWVWVEASAVPLRDGGEVIgVLGIVRDITERKRAE 255
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
751-872 7.54e-03

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: 37.33  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 751 GLRVLLAEDNDLNaeiacellaeaglVVERAGDGAEACVMFEASKIgyfDAVLMDVQMPNMNGYEATRCIREldrEDADA 830
Cdd:cd19931    13 GIKQLIELDPDFT-------------VVGEASSGEEGIELAERLDP---DLILLDLNMKGMSGLDTLKALRE---EGVSA 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2575951464 831 VPIIAMSANAfAEDVSASLASGMNAHLSKPIDMRRVLATLIK 872
Cdd:cd19931    74 RIVILTVSDA-EDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
754-860 9.85e-03

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: 36.33  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2575951464 754 VLLAEDNDLNAEIACELLAEAGLVVERAGDgaeACVMFEASKIGYFDAVLMDVQMPNMNGYEATRCIRELdREDadaVPI 833
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGN---AATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIKKA-RPD---LPI 73
                          90       100
                  ....*....|....*....|....*...
gi 2575951464 834 IAMSA-NAFAEDVSASlASGMNAHLSKP 860
Cdd:cd19928    74 IVMSAqNTLMTAVKAA-ERGAFEYLPKP 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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