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Conserved domains on  [gi|18398532|ref|NP_565424|]
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histidine kinase 1 [Arabidopsis thaliana]

Protein Classification

hybrid sensor histidine kinase/response regulator( domain architecture ID 12788382)

two-component hybrid sensor histidine kinase/response regulator receives the signal from the sensor partner in two-component systems through its receiver (REC) domain and functions as a protein kinase that phosphorylates a target protein in response to various signals

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];
478-759 3.08e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 221.32  E-value: 3.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  478 LRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDdcLSNEQYATVTQIRKCSTALLRLLNNILD 557
Cdd:COG0642   89 LLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLD 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  558 LSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTTGHII 637
Cdd:COG0642  167 LSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDD-LPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTV 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  638 lrgwceninslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADPS 717
Cdd:COG0642  246 ---------------TVSVRREGDR-------------------------VRISVEDTGPGIPPEDLERIFEPFFRTDPS 285
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18398532  718 ttRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG0642  286 --RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
485-1184 5.53e-62

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 229.35  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLD-ARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDcLSNEQYATVTQIRKCSTALLRLLNNILDLSKVES 563
Cdd:PRK11107  278 ELDlAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   564 GKLVLEEAEFDLgRE-LEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILRgwc 642
Cdd:PRK11107  357 GKLVLENIPFSL-REtLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDIL--- 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   643 eninslhdemsvsvdrrkpwapmktkqVQHRNHlqksckNANKMVLWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTH 722
Cdd:PRK11107  433 ---------------------------VELRAL------SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRH 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   723 GGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVdQNIQPDFSKY-GLVVMLSMYGSTARMITSKWLRK 801
Cdd:PRK11107  480 GGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNP-IIDGLPTDCLaGKRLLYVEPNSAAAQATLDILSE 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   802 HGIATVEASDWNELTQIIRDLLETGSRDNSFDSQHNISDPLRAelsniveiknpvfvivvdigVLDLTTNIwkeqlnyld 881
Cdd:PRK11107  559 TPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAK--------------------AKSMTDFL--------- 609
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   882 rfsnkakfawLLKHD-TSNTVKTELRRKGHVMMVNKPLYKAKMIQILEAviknrkrglcndlrnrgngsdeshdcleidp 960
Cdd:PRK11107  610 ----------ILALPcHEQVLAEQLKQDGADACLSKPLSHTRLLPALLE------------------------------- 648
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   961 tqfdtcssddssetsgekqvdksvkPSTLHSPvlknylidattsndDSTSASMTQKNPeeedwkdrlysgialdgknqks 1040
Cdd:PRK11107  649 -------------------------PCHHKQP--------------PLLPPTDESRLP---------------------- 667
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1041 legIRILLAEDTPV-LQRVATiMLEKMGATVTAVWDGQQAVdslnyksinAQAptEEHksfeeetankvttretslrnss 1119
Cdd:PRK11107  668 ---LTVMAVDDNPAnLKLIGA-LLEEQVEHVVLCDSGHQAV---------EQA--KQR---------------------- 710
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1120 PYDLILMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:PRK11107  711 PFDLILMDIQMPGMDGIRACELIRQLPHNQ--NTPIIAVTAHAMAGERERLLSAGMDDYLAKPID 773
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
478-759 3.08e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 221.32  E-value: 3.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  478 LRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDdcLSNEQYATVTQIRKCSTALLRLLNNILD 557
Cdd:COG0642   89 LLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLD 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  558 LSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTTGHII 637
Cdd:COG0642  167 LSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDD-LPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTV 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  638 lrgwceninslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADPS 717
Cdd:COG0642  246 ---------------TVSVRREGDR-------------------------VRISVEDTGPGIPPEDLERIFEPFFRTDPS 285
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18398532  718 ttRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG0642  286 --RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
485-1184 5.53e-62

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 229.35  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLD-ARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDcLSNEQYATVTQIRKCSTALLRLLNNILDLSKVES 563
Cdd:PRK11107  278 ELDlAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   564 GKLVLEEAEFDLgRE-LEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILRgwc 642
Cdd:PRK11107  357 GKLVLENIPFSL-REtLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDIL--- 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   643 eninslhdemsvsvdrrkpwapmktkqVQHRNHlqksckNANKMVLWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTH 722
Cdd:PRK11107  433 ---------------------------VELRAL------SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRH 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   723 GGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVdQNIQPDFSKY-GLVVMLSMYGSTARMITSKWLRK 801
Cdd:PRK11107  480 GGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNP-IIDGLPTDCLaGKRLLYVEPNSAAAQATLDILSE 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   802 HGIATVEASDWNELTQIIRDLLETGSRDNSFDSQHNISDPLRAelsniveiknpvfvivvdigVLDLTTNIwkeqlnyld 881
Cdd:PRK11107  559 TPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAK--------------------AKSMTDFL--------- 609
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   882 rfsnkakfawLLKHD-TSNTVKTELRRKGHVMMVNKPLYKAKMIQILEAviknrkrglcndlrnrgngsdeshdcleidp 960
Cdd:PRK11107  610 ----------ILALPcHEQVLAEQLKQDGADACLSKPLSHTRLLPALLE------------------------------- 648
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   961 tqfdtcssddssetsgekqvdksvkPSTLHSPvlknylidattsndDSTSASMTQKNPeeedwkdrlysgialdgknqks 1040
Cdd:PRK11107  649 -------------------------PCHHKQP--------------PLLPPTDESRLP---------------------- 667
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1041 legIRILLAEDTPV-LQRVATiMLEKMGATVTAVWDGQQAVdslnyksinAQAptEEHksfeeetankvttretslrnss 1119
Cdd:PRK11107  668 ---LTVMAVDDNPAnLKLIGA-LLEEQVEHVVLCDSGHQAV---------EQA--KQR---------------------- 710
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1120 PYDLILMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:PRK11107  711 PFDLILMDIQMPGMDGIRACELIRQLPHNQ--NTPIIAVTAHAMAGERERLLSAGMDDYLAKPID 773
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
477-775 4.13e-49

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: 189.99  E-value: 4.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    477 KLRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDiLISDDCLSNEQYATVTQIRKCSTALLRLLNNIL 556
Cdd:TIGR02956  442 RLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    557 DLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHI 636
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSV 600
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    637 ILRgwceniNSLHDEMSvsvdrrkpwapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADp 716
Cdd:TIGR02956  601 VLR------VSLNDDSS----------------------------------LLFEVEDTGCGIAEEEQATLFDAFTQAD- 639
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532    717 sTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLIL--STPDTVDQNIQPDF 775
Cdd:TIGR02956  640 -GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLtrGKPAEDSATLTVID 699
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1046-1192 7.39e-46

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: 160.33  E-value: 7.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLIL 1125
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLK---------------------------------EEPFDLVL 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEiGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17546   48 MDLQMPVMDGLEATRRIRELE-GGGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK15347 PRK15347
two component system sensor kinase;
384-762 2.16e-43

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 171.75  E-value: 2.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   384 QWLEKTYGSKRPHVVHA-----ENVKLGDQRYYIDSFYLNLKRLPIVG---VVIIPRKFIMgkvdERAFKTLIILISASV 455
Cdd:PRK15347  228 ELLPFSTIPLSSNQLQKilnqlENVKLHDGWQQIPDYLVLRTQLKGPGwqqVTLYPRRNLA----NEALKPALQQLPFAL 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   456 CI-FFIGCVCILILTNGVSK--------------------------------------------------EMKLrAELIR 484
Cdd:PRK15347  304 LIlVLLTSVLFLLLRRYLAKplwrfvdiinktgpaaleprlpenrldelgsiakaynqlldtlneqydtlENKV-AERTQ 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLD-ARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVES 563
Cdd:PRK15347  383 ALAeAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELL-QNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIES 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   564 GKLVLEEAEFDLgreLEgLVD--MFSVQCINHNVETVLD--LSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILR 639
Cdd:PRK15347  462 GQMTLSLEETAL---LP-LLDqaMLTIQGPAQSKSLTLRtfVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLR 537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   640 GWCENinslhdemsvsvdrrkpwapmktkqvQHrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADpstt 719
Cdd:PRK15347  538 VKRHE--------------------------QQ---------------LCFTVEDTGCGIDIQQQQQIFTPFYQAD---- 572
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 18398532   720 rTH-GGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILS 762
Cdd:PRK15347  573 -THsQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLN 615
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1040-1195 3.01e-39

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: 141.91  E-value: 3.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1040 SLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSS 1119
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLR---------------------------------AG 48
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1120 PYDLILMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:COG0784   49 PPDLILLDINMPGMDGLELLRRIRALPRLP--DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
618-761 2.39e-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: 118.75  E-value: 2.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  618 QIFANLISNSIKFTTTGHIILRGWCENINSLHDemsvsvdrrkpwapmktkqvqhrnhlqkscknankmVLWFEVDDTGC 697
Cdd:cd16922    3 QILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGV------------------------------------QLRFSVEDTGI 46
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532  698 GIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLIL 761
Cdd:cd16922   47 GIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
611-762 4.12e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 101.19  E-value: 4.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532     611 GDSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWF 690
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRI---------------TVTLERDGDH-------------------------VEI 40
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532     691 EVDDTGCGIDPSKWDSVFESFEQADPsTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILS 762
Cdd:smart00387   41 TVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1046-1192 2.10e-23

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 96.07  E-value: 2.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnsspYDLIL 1125
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL-----------KEER----------------------PDLIL 47
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532   1126 MDCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:pfam00072   48 LDINMPGMDGLELLKRIRR----RDPTTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
499-743 5.91e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 5.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   499 KSQFLANMSHELRTPMAAVIGLLDILisDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVLEEAEFDLGRE 578
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   579 LEGLVDMFSVQCINHNVETVLDLSDDMpaLVRGDSARLVQIFANLISNSIKFTTTGhiilrgwceniNSLHdemsVSVDR 658
Cdd:NF012163  318 LEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSG-----------GSLH----ISASQ 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   659 RKpwapmktKQVQhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNK 738
Cdd:NF012163  381 RP-------KEVT------------------LTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQA 435

                  ....*
gi 18398532   739 MGGEI 743
Cdd:NF012163  436 HGGTL 440
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
611-759 1.10e-20

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: 88.19  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    611 GDSARLVQIFANLISNSIKFTTTGhiilrgwceninslhDEMSVSVDRrkpwapmktkqvqhrnhlqkscknanKMVLWF 690
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKA---------------GEITVTLSE--------------------------GGELTL 39
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532    691 EVDDTGCGIDPSKWDSVFESFEQADpstTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:pfam02518   40 TVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
485-753 1.20e-18

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 91.35  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLDARRRaeassnyksQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYA----TVTQ------IrkcstallRLLNN 554
Cdd:NF033092  367 KIEQERR---------EFVANVSHELRTPLTTMRSYLEAL-ADGAWKDPELAprflGVTQnetermI--------RLVND 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   555 ILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTT- 633
Cdd:NF033092  429 LLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKR-DLWVEIDTDKITQVLDNIISNAIKYSPEg 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   634 GHIILRgwcenINSLHDEMSVSvdrrkpwapmktkqvqhrnhlqkscknankmvlwfeVDDTGCGIDPSKWDSVFESFEQ 713
Cdd:NF033092  508 GTITFR-----LLETHNRIIIS------------------------------------ISDQGLGIPKKDLDKIFDRFYR 546
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 18398532   714 ADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:NF033092  547 VDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGT 586
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
483-759 8.08e-14

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 75.45  E-value: 8.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   483 IRQLdarrraEASSNYKSQFLANMSHELRTPmaavigLLDILISDDCLSNEQYATVTQIRKcSTALL--------RLLNN 554
Cdd:NF040691  261 IRQL------EELSRLQQRFVSDVSHELRTP------LTTIRMAADVIHDSRDDFDPATAR-SAELLhteldrfeSLLSD 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   555 ILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLsDDMPALVRGDSARLVQIFANLISNSIKFTTTG 634
Cdd:NF040691  328 LLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGK 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   635 HIILRgwcenINSlhDEMSVSVdrrkpwapmktkqvqhrnhlqkscknankmvlwfEVDDTGCGIDPSKWDSVFESFEQA 714
Cdd:NF040691  407 PVVVT-----VAQ--DDTAVAV----------------------------------TVRDHGVGLKPGEVALVFDRFWRA 445
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 18398532   715 DPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:NF040691  446 DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
504-750 1.49e-10

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 64.25  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   504 ANMSHELRTPMAAVIGLL-----DILISDDCLSNEQYATVTQirkcstaLLRLLNNILDLSKVESGKLVLEEAEFDLGRE 578
Cdd:NF012226  143 AAIAHELRTPITILQGRLqgildGVFEPDPALFKSLLNQVEG-------LSHLVEDLRTLSLVENQQLRLNYESVDLKDS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   579 LEGLVDMFSVQCINHNVETVLDLSDDmpaLVRGDSARLVQIFANLISNSIKFTTTGHIILRgwceninslhdemsvsvdr 658
Cdd:NF012226  216 IEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKIS------------------- 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   659 rkpwapmktkqvqhrnhlqkSCKNANKMVLWFEvdDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNK 738
Cdd:NF012226  274 --------------------SSVIQDDWILQIE--DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIA 331
                         250
                  ....*....|..
gi 18398532   739 MGGEIKVVQKNG 750
Cdd:NF012226  332 HKGSIEYSNSQG 343
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
478-759 3.08e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 221.32  E-value: 3.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  478 LRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDdcLSNEQYATVTQIRKCSTALLRLLNNILD 557
Cdd:COG0642   89 LLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLD 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  558 LSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTTGHII 637
Cdd:COG0642  167 LSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDD-LPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTV 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  638 lrgwceninslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADPS 717
Cdd:COG0642  246 ---------------TVSVRREGDR-------------------------VRISVEDTGPGIPPEDLERIFEPFFRTDPS 285
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 18398532  718 ttRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG0642  286 --RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
485-1184 5.53e-62

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 229.35  E-value: 5.53e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLD-ARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDcLSNEQYATVTQIRKCSTALLRLLNNILDLSKVES 563
Cdd:PRK11107  278 ELDlAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEA 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   564 GKLVLEEAEFDLgRE-LEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILRgwc 642
Cdd:PRK11107  357 GKLVLENIPFSL-REtLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDIL--- 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   643 eninslhdemsvsvdrrkpwapmktkqVQHRNHlqksckNANKMVLWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTH 722
Cdd:PRK11107  433 ---------------------------VELRAL------SNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRH 479
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   723 GGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVdQNIQPDFSKY-GLVVMLSMYGSTARMITSKWLRK 801
Cdd:PRK11107  480 GGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNP-IIDGLPTDCLaGKRLLYVEPNSAAAQATLDILSE 558
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   802 HGIATVEASDWNELTQIIRDLLETGSRDNSFDSQHNISDPLRAelsniveiknpvfvivvdigVLDLTTNIwkeqlnyld 881
Cdd:PRK11107  559 TPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPLTMLHERLAK--------------------AKSMTDFL--------- 609
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   882 rfsnkakfawLLKHD-TSNTVKTELRRKGHVMMVNKPLYKAKMIQILEAviknrkrglcndlrnrgngsdeshdcleidp 960
Cdd:PRK11107  610 ----------ILALPcHEQVLAEQLKQDGADACLSKPLSHTRLLPALLE------------------------------- 648
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   961 tqfdtcssddssetsgekqvdksvkPSTLHSPvlknylidattsndDSTSASMTQKNPeeedwkdrlysgialdgknqks 1040
Cdd:PRK11107  649 -------------------------PCHHKQP--------------PLLPPTDESRLP---------------------- 667
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1041 legIRILLAEDTPV-LQRVATiMLEKMGATVTAVWDGQQAVdslnyksinAQAptEEHksfeeetankvttretslrnss 1119
Cdd:PRK11107  668 ---LTVMAVDDNPAnLKLIGA-LLEEQVEHVVLCDSGHQAV---------EQA--KQR---------------------- 710
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1120 PYDLILMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:PRK11107  711 PFDLILMDIQMPGMDGIRACELIRQLPHNQ--NTPIIAVTAHAMAGERERLLSAGMDDYLAKPID 773
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
478-759 4.37e-57

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 202.86  E-value: 4.37e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  478 LRAELIRQLDARRRAEASsnyKSQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYA-TVTQIRKCSTALLRLLNNIL 556
Cdd:COG5002  147 LLAAVERDITELERLEQM---RREFVANVSHELRTPLTSIRGYLELLLDGAADDPEERReYLEIILEEAERLSRLVNDLL 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  557 DLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTTGHI 636
Cdd:COG5002  224 DLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPED-PLLVLGDPDRLEQVLTNLLDNAIKYTPEGGT 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  637 IlrgwceninslhdemSVSVDRRKPWApmktkqvqhrnhlqkscknankmvlWFEVDDTGCGIDPSKWDSVFESFEQADP 716
Cdd:COG5002  303 I---------------TVSLREEDDQV-------------------------RISVRDTGIGIPEEDLPRIFERFYRVDK 342
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 18398532  717 STTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG5002  343 SRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
487-759 3.39e-55

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 192.04  E-value: 3.39e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  487 DARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYAT-VTQIRKCSTALLRLLNNILDLSKVESGK 565
Cdd:COG2205    4 EALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERRElLEIIRESAERLLRLIEDLLDLSRLESGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  566 LVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPaLVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceni 645
Cdd:COG2205   84 LSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGGTI-------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  646 nslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADpsTTRTHGGT 725
Cdd:COG2205  155 -------TISARREGDG-------------------------VRISVSDNGPGIPEEELERIFERFYRGD--NSRGEGGT 200
                        250       260       270
                 ....*....|....*....|....*....|....
gi 18398532  726 GLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG2205  201 GLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTL 234
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
477-775 4.13e-49

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: 189.99  E-value: 4.13e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    477 KLRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDiLISDDCLSNEQYATVTQIRKCSTALLRLLNNIL 556
Cdd:TIGR02956  442 RLNAEVKNHAKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDIL 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    557 DLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHI 636
Cdd:TIGR02956  521 DYSKIEAGHLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSV 600
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    637 ILRgwceniNSLHDEMSvsvdrrkpwapmktkqvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADp 716
Cdd:TIGR02956  601 VLR------VSLNDDSS----------------------------------LLFEVEDTGCGIAEEEQATLFDAFTQAD- 639
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532    717 sTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLIL--STPDTVDQNIQPDF 775
Cdd:TIGR02956  640 -GRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLtrGKPAEDSATLTVID 699
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1046-1192 7.39e-46

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: 160.33  E-value: 7.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLIL 1125
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLK---------------------------------EEPFDLVL 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEiGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17546   48 MDLQMPVMDGLEATRRIRELE-GGGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK15347 PRK15347
two component system sensor kinase;
384-762 2.16e-43

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 171.75  E-value: 2.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   384 QWLEKTYGSKRPHVVHA-----ENVKLGDQRYYIDSFYLNLKRLPIVG---VVIIPRKFIMgkvdERAFKTLIILISASV 455
Cdd:PRK15347  228 ELLPFSTIPLSSNQLQKilnqlENVKLHDGWQQIPDYLVLRTQLKGPGwqqVTLYPRRNLA----NEALKPALQQLPFAL 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   456 CI-FFIGCVCILILTNGVSK--------------------------------------------------EMKLrAELIR 484
Cdd:PRK15347  304 LIlVLLTSVLFLLLRRYLAKplwrfvdiinktgpaaleprlpenrldelgsiakaynqlldtlneqydtlENKV-AERTQ 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLD-ARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVES 563
Cdd:PRK15347  383 ALAeAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELL-QNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIES 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   564 GKLVLEEAEFDLgreLEgLVD--MFSVQCINHNVETVLD--LSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILR 639
Cdd:PRK15347  462 GQMTLSLEETAL---LP-LLDqaMLTIQGPAQSKSLTLRtfVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLR 537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   640 GWCENinslhdemsvsvdrrkpwapmktkqvQHrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADpstt 719
Cdd:PRK15347  538 VKRHE--------------------------QQ---------------LCFTVEDTGCGIDIQQQQQIFTPFYQAD---- 572
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 18398532   720 rTH-GGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILS 762
Cdd:PRK15347  573 -THsQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLN 615
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
473-834 6.05e-40

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 160.84  E-value: 6.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   473 SKEMKLRAELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYATVTQIRKCSTALLRLL 552
Cdd:PRK11466  418 ARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLL-ADNPALNAQRDDLRAITDSGESLLTIL 496
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   553 NNILDLSKVESG--KLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKF 630
Cdd:PRK11466  497 NDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRF 576
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   631 TTTGHIILRGWCeninslhDEMSvsvdrrkpWapmktkqvqhrnhlqkscknankmvlWFEVDDTGCGIDPSKWDSVFES 710
Cdd:PRK11466  577 TDEGSIVLRSRT-------DGEQ--------W--------------------------LVEVEDSGCGIDPAKLAEIFQP 615
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   711 FEQAdpstTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLIL-----STPDTVDQNIQPDfskyGLVVMLS 785
Cdd:PRK11466  616 FVQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLrvataPVPKTVNQAVRLD----GLRLLLI 687
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 18398532   786 MYGSTARMITSKWLRKHGIATVEASDWNEltqiirdLLETGSRDNSFDS 834
Cdd:PRK11466  688 EDNPLTQRITAEMLNTSGAQVVAVGNAAQ-------ALETLQNSEPFAA 729
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1040-1195 3.01e-39

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: 141.91  E-value: 3.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1040 SLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSS 1119
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLR---------------------------------AG 48
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1120 PYDLILMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:COG0784   49 PPDLILLDINMPGMDGLELLRRIRALPRLP--DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
492-1183 1.47e-36

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 150.12  E-value: 1.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   492 AEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDDcLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVLEEA 571
Cdd:PRK10841  440 AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKE-LPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPR 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   572 EFDlGRELeglvdmfsvqcINHNVETVLDL------------SDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILR 639
Cdd:PRK10841  519 EFS-PREV-----------INHITANYLPLvvkkrlglycfiEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLH 586
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   640 gwceninslhdemsVSVDrrkpwapmktkqvqhrnhlqkscknanKMVLWFEVDDTGCGIDPSKWDSVFESFEQADPSTT 719
Cdd:PRK10841  587 --------------VRVD---------------------------GDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQ 625
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   720 RTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVDQNIQPDFSkyGLVVMLSMYGSTARMITSKWL 799
Cdd:PRK10841  626 RNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQ--GKRCWLAVRNASLEQFLETLL 703
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   800 RKHGIATVEASDwneltqiirdlLETGSRDnsfdsqhnisdplraelsniveiknpvfVIVVDigvldlttniwkeqlny 879
Cdd:PRK10841  704 QRSGIQVQRYEG-----------QEPTPED----------------------------VLITD----------------- 727
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   880 ldrfsnkakfawllkhdtsntvktelrrkgHVMMVNKPLYkakmiqileAVIKnrkrglcndLRNRGNGSDEshdclEID 959
Cdd:PRK10841  728 ------------------------------DPVQKKWQGR---------AVIT---------FCRRHIGIPL-----EIA 754
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   960 PTQFdTCSsddssetsgekqvdksvkPSTLHS-PVLKNYLIDATTSNDDSTSASMTQKnpeeedwkdrlysgialdgKNQ 1038
Cdd:PRK10841  755 PGEW-VHS------------------TATPHElPALLARIYRIELESDDSANALPSTD-------------------KAV 796
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1039 KSLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGqqaVDSLNYKSINaqapteehksfeeetankvttretslrns 1118
Cdd:PRK10841  797 SDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDG---VDALNVLSKN----------------------------- 844
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1119 sPYDLILMDCQMPKMDGYEATKAIRraEIGteLHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:PRK10841  845 -HIDIVLTDVNMPNMDGYRLTQRLR--QLG--LTLPVIGVTANALAEEKQRCLEAGMDSCLSKPV 904
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
483-753 3.97e-32

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: 128.48  E-value: 3.97e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    483 IRQLDARRRaeassnyksQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYA-TVTQIRKCSTALLRLLNNILDLSKV 561
Cdd:TIGR02966  107 LRRLEQMRR---------DFVANVSHELRTPLTVLRGYLETLADGPDEDPEEWNrALEIMLEQSQRMQSLVEDLLTLSRL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    562 ESGKLVLEEAEFDLGRELEGLVDmfSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTG-HIILRg 640
Cdd:TIGR02966  178 ESAASPLEDEPVDMPALLDHLRD--EAEALSQGKNHQITFEIDGGVDVLGDEDELRSAFSNLVSNAIKYTPEGgTITVR- 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    641 wceninslhdemsvsvdrrkpWAPMKTKQVqhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFESFEQADPSTTR 720
Cdd:TIGR02966  255 ---------------------WRRDGGGAE-------------------FSVTDTGIGIAPEHLPRLTERFYRVDKSRSR 294
                          250       260       270
                   ....*....|....*....|....*....|...
gi 18398532    721 THGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:TIGR02966  295 DTGGTGLGLAIVKHVLSRHHARLEIESELGKGS 327
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
618-761 2.39e-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: 118.75  E-value: 2.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  618 QIFANLISNSIKFTTTGHIILRGWCENINSLHDemsvsvdrrkpwapmktkqvqhrnhlqkscknankmVLWFEVDDTGC 697
Cdd:cd16922    3 QILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGV------------------------------------QLRFSVEDTGI 46
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532  698 GIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLIL 761
Cdd:cd16922   47 GIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
445-770 3.64e-30

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: 126.24  E-value: 3.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  445 KTLIILISASVCIFFIGCVCILILTNGVSKEMKLrAELIRQLDARRRAeassnykSQFLANMSHELRTPMAAVIGLLDIL 524
Cdd:COG5809  224 RWRLLEASGAPIKKNGEVDGIVIIFRDITERKKL-EELLRKSEKLSVV-------GELAAGIAHEIRNPLTSLKGFIQLL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  525 ISDDCLSNEQYATVtqIRKCSTALLRLLNNILDLSKVESGKlvleEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDD 604
Cdd:COG5809  296 KDTIDEEQKTYLDI--MLSELDRIESIISEFLVLAKPQAIK----YEPKDLNTLIEEVIPLLQPQALLKNVQIELELEDD 369
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  605 MPaLVRGDSARLVQIFANLISNSIKFTTTGhiilrGwceninslhdemSVSVDRRkpwapmktkqvqhrnhlqksCKNAN 684
Cdd:COG5809  370 IP-DILGDENQLKQVFINLLKNAIEAMPEG-----G------------NITIETK--------------------AEDDD 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  685 KMVlwFEVDDTGCGIDPSKWDSVFESFeqadpSTTRtHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTP 764
Cdd:COG5809  412 KVV--ISVTDEGCGIPEERLKKLGEPF-----YTTK-EKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLS 483

                 ....*.
gi 18398532  765 DTVDQN 770
Cdd:COG5809  484 EQVSMN 489
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1045-1192 1.38e-29

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: 116.16  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQ---------------------------------EHRPDLI 49
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:COG3706   50 LLDLEMPDMDGLELCRRLRADPRTA--DIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
412-759 2.90e-29

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 123.74  E-value: 2.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  412 IDSFYLNLKRLPIVGVVIIPRKFIMGKVDERAFKTLIILISASVCIFFIGCVCILILTNGVSKEMKLRAELIRQLDARRR 491
Cdd:COG4251  194 LLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTA 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  492 A-EASSNYKSQFLANMSHELRTPMAAVIGLLDILISD--DCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVL 568
Cdd:COG4251  274 ElERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDygDKLDEEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEF 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  569 EEaeFDLGRELEGLVDMFSVQCINHNVETVLDlsdDMPAlVRGDSARLVQIFANLISNSIKFT---TTGHIilrgwceni 645
Cdd:COG4251  354 EP--VDLNELLEEVLEDLEPRIEERGAEIEVG---PLPT-VRGDPTLLRQVFQNLISNAIKYSrpgEPPRI--------- 418
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  646 nslhdemSVSVDRRKPWApmktkqvqhrnhlqkscknankmvlWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRthGGT 725
Cdd:COG4251  419 -------EIGAEREGGEW-------------------------VFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEY--EGT 464
                        330       340       350
                 ....*....|....*....|....*....|....
gi 18398532  726 GLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG4251  465 GIGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
445-759 3.04e-29

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 120.72  E-value: 3.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  445 KTLIILISASVCIFFIGCVCILILTNGVSKEMKLRAELIRqldaRRRAEASSnyksQFLANMSHELRTPMAAVIGLLDIL 524
Cdd:COG3852   89 EERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRR----AEKLAAVG----ELAAGLAHEIRNPLTGIRGAAQLL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  525 ISDdcLSNEQYATVTQ-IRKCSTALLRLLNNILDLSKVESGKLvleeAEFDLGRELEGLVDMFSVQcINHNVETVLDLSD 603
Cdd:COG3852  161 ERE--LPDDELREYTQlIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLERVLELLRAE-APKNIRIVRDYDP 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  604 DMPAlVRGDSARLVQIFANLISNSIK-FTTTGHIILRGWCENINSLHDEmsvsvdrrkpwapmktkqvQHRNHLQksckn 682
Cdd:COG3852  234 SLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQVTLGGL-------------------RPRLYVR----- 288
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532  683 ankmvlwFEVDDTGCGIDPSKWDSVFESFEqadpsTTRThGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG3852  289 -------IEVIDNGPGIPEEILDRIFEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYL 352
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
484-753 2.22e-27

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 120.05  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   484 RQLDARRRA----EASSNYKSQFLANMSHELRTPMAAVIGLLDILIsDDCLSNEQYATVTQIRKCSTALLRLLNNILDLS 559
Cdd:PRK11091  264 RDITERKRYqdalEKASRDKTTFISTISHELRTPLNGIVGLSRILL-DTELTAEQRKYLKTIHVSAITLGNIFNDIIDMD 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   560 KVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPALVRGDSARLVQIFANLISNSIKFTTTGHIILR 639
Cdd:PRK11091  343 KMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVR 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   640 GWCENINSLHdemsvsvdrrkpwapmktkqvqhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFESFEQADPSTT 719
Cdd:PRK11091  423 VRYEEGDMLT----------------------------------------FEVEDSGIGIPEDELDKIFAMYYQVKDSHG 462
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 18398532   720 RTHG-GTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:PRK11091  463 GKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGS 497
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
480-759 6.71e-27

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 113.74  E-value: 6.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  480 AELIRQLDARRRAEA----SSNYKS--QFLANMSHELRTPMAAVIGLLDIL---ISDDCLSNEQYATVTQIRKCSTALLR 550
Cdd:COG4191  117 TELERAEEELRELQEqlvqSEKLAAlgELAAGIAHEINNPLAAILGNAELLrrrLEDEPDPEELREALERILEGAERAAE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  551 LLNNILDLSKVESGKLVleeaEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPaLVRGDSARLVQIFANLISNSIkf 630
Cdd:COG4191  197 IVRSLRAFSRRDEEERE----PVDLNELIDEALELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINAI-- 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  631 tttghiilrgwceninslhDEMSVSVDRRkpwapmktkqvqhrnhLQKSCKNANKMVLwFEVDDTGCGIDPSKWDSVFES 710
Cdd:COG4191  270 -------------------DAMEEGEGGR----------------ITISTRREGDYVV-ISVRDNGPGIPPEVLERIFEP 313
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18398532  711 FeqadpSTTRTHG-GTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG4191  314 F-----FTTKPVGkGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITL 358
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1045-1192 8.73e-27

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: 106.09  E-value: 8.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqapteehksfeeetankvttretslRNSSPyDLI 1124
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIA--------------------------------RKEKP-DLI 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1125 LMDCQMPKMDGYEATKAIRrAEIGTElHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17548   48 LMDIQLPGMDGLEATRLLK-EDPATR-DIPVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETV 113
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1045-1195 2.70e-26

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: 107.73  E-value: 2.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:COG0745    3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLE---------------------------------EERPDLI 49
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:COG0745   50 LLDLMLPGMDGLEVCRRLRARPS----DIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRAL 116
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
611-762 4.12e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 101.19  E-value: 4.12e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532     611 GDSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemSVSVDRRKPWapmktkqvqhrnhlqkscknankmvLWF 690
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRI---------------TVTLERDGDH-------------------------VEI 40
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532     691 EVDDTGCGIDPSKWDSVFESFEQADPsTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILS 762
Cdd:smart00387   41 TVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1046-1192 2.10e-23

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 96.07  E-value: 2.10e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnsspYDLIL 1125
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL-----------KEER----------------------PDLIL 47
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532   1126 MDCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:pfam00072   48 LDINMPGMDGLELLKRIRR----RDPTTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
506-759 3.00e-22

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: 101.19  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  506 MSHELRTPMAAVIGLLDILISDDCLSNEQYATVTQ-----IRKCSTALLRLLNNILDLSKVESGKLvleeAEFDLGRELE 580
Cdd:COG5000  208 IAHEIKNPLTPIQLSAERLRRKLADKLEEDREDLEraldtIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLR 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  581 GLVDMFSVQCINHNVETVLDLSDDMPaLVRGDSARLVQIFANLISNSIKFT-TTGHIIlrgwceninslhdemsVSVDRR 659
Cdd:COG5000  284 EVLALYEPALKEKDIRLELDLDPDLP-EVLADRDQLEQVLINLLKNAIEAIeEGGEIE----------------VSTRRE 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  660 KPWApmktkqvqhrnhlqkscknankmvlWFEVDDTGCGIDPSKWDSVFESFEqadpsTTRTHGgTGLGLCIVRNLVNKM 739
Cdd:COG5000  347 DGRV-------------------------RIEVSDNGPGIPEEVLERIFEPFF-----TTKPKG-TGLGLAIVKKIVEEH 395
                        250       260
                 ....*....|....*....|
gi 18398532  740 GGEIKVVQKNGLGTLMRLYL 759
Cdd:COG5000  396 GGTIELESRPGGGTTFTIRL 415
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
481-811 2.45e-21

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 100.96  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   481 ELIRQLDARR-RAEASSNYKSQFLANMSHELRTPMAAVIGLLDiLISDDCLSNEQYATVTQIRKCS-TALLRLLNNILDL 558
Cdd:PRK09959  693 DLIHALEVERnKAINATVAKSQFLATMSHEIRTPISSIMGFLE-LLSGSGLSKEQRVEAISLAYATgQSLLGLIGEILDV 771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   559 SKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVetVLDLSDDMP--ALVRGDSARLVQIFANLISNSIKFTTTGHI 636
Cdd:PRK09959  772 DKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSI--ALSCSSTFPdhYLVKIDPQAFKQVLSNLLSNALKFTTEGAV 849
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   637 ILrgwceninslhdemsvsvdrrkpwapmkTKQVQHRNHlqkscknaNKMVLWFEVDDTGCGIDPSKWDSVFESFEQAdp 716
Cdd:PRK09959  850 KI----------------------------TTSLGHIDD--------NHAVIKMTIMDSGSGLSQEEQQQLFKRYSQT-- 891
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   717 STTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLmrlyLILSTPDTVDQNI--------QPDFSKYGLVVMLSMYG 788
Cdd:PRK09959  892 SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTT----FTITIPVEISQQVatveakaeQPITLPEKLSILIADDH 967
                         330       340
                  ....*....|....*....|...
gi 18398532   789 STARMITSKWLRKHGIATVEASD 811
Cdd:PRK09959  968 PTNRLLLKRQLNLLGYDVDEATD 990
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
499-743 5.91e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 97.59  E-value: 5.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   499 KSQFLANMSHELRTPMAAVIGLLDILisDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVLEEAEFDLGRE 578
Cdd:NF012163  240 RRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLVPL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   579 LEGLVDMFSVQCINHNVETVLDLSDDMpaLVRGDSARLVQIFANLISNSIKFTTTGhiilrgwceniNSLHdemsVSVDR 658
Cdd:NF012163  318 LEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSG-----------GSLH----ISASQ 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   659 RKpwapmktKQVQhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNK 738
Cdd:NF012163  381 RP-------KEVT------------------LTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQA 435

                  ....*
gi 18398532   739 MGGEI 743
Cdd:NF012163  436 HGGTL 440
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
500-750 6.83e-21

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: 97.46  E-value: 6.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    500 SQFLANMSHELRTPMAAVIGLLDILISDDcLSNEQYATVTQirkcSTA-----LLRLLNNILDLSKVESGKLVLEEAEFD 574
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVALSQP-RTGEEYREVLE----SNLeelerLSRMVSDMLFLARADNGQLALERVRLD 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    575 LGRELEGLVDMFSVQCINHNVEtvLDLSDDmpALVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemSV 654
Cdd:TIGR01386  317 LAAELAKVAEYFEPLAEERGVR--IRVEGE--GLVRGDPQMFRRAISNLLSNALRHTPDGGTI---------------TV 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    655 SVDRRkpwapmktkqvqhRNHLQKScknankmvlwfeVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRN 734
Cdd:TIGR01386  378 RIERR-------------SDEVRVS------------VSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRS 432
                          250
                   ....*....|....*.
gi 18398532    735 LVNKMGGEIKVVQKNG 750
Cdd:TIGR01386  433 IMEAHGGRASAESPDG 448
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
611-759 1.10e-20

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: 88.19  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    611 GDSARLVQIFANLISNSIKFTTTGhiilrgwceninslhDEMSVSVDRrkpwapmktkqvqhrnhlqkscknanKMVLWF 690
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKA---------------GEITVTLSE--------------------------GGELTL 39
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532    691 EVDDTGCGIDPSKWDSVFESFEQADpstTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:pfam02518   40 TVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTL 105
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1046-1184 1.30e-20

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: 88.28  E-value: 1.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTP-VLQRVATiMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:cd17580    1 ILVVDDNEdAAEMLAL-LLELEGAEVTTAHSGEEALEAAQ---------------------------------RFRPDVI 46
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd17580   47 LSDIGMPGMDGYELARRLRELPWLA--NTPAIALTGYGQPEDRERALEAGFDAHLVKPVD 104
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1045-1195 5.22e-20

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: 90.22  E-value: 5.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHksfeeetankvttretslrnssPYDLI 1124
Cdd:COG3437    8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL-----------LEA----------------------PPDLI 54
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGteLHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:COG3437   55 LLDVRMPGMDGFELLRLLRADPST--RDIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNA 123
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1047-1182 6.42e-19

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: 83.05  E-value: 6.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1047 LLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLILM 1126
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLR---------------------------------EERPDLVLL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1127 DCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd00156   48 DLMMPGMDGLELLRKLRE----LPPDIPVIVLTAKADEEDAVRALELGADDYLVKP 99
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
485-753 1.20e-18

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 91.35  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   485 QLDARRRaeassnyksQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYA----TVTQ------IrkcstallRLLNN 554
Cdd:NF033092  367 KIEQERR---------EFVANVSHELRTPLTTMRSYLEAL-ADGAWKDPELAprflGVTQnetermI--------RLVND 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   555 ILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTT- 633
Cdd:NF033092  429 LLQLSRMDSKDYKLNKEWVNFNEFFNYIIDRFEMILKNKNITFKREFPKR-DLWVEIDTDKITQVLDNIISNAIKYSPEg 507
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   634 GHIILRgwcenINSLHDEMSVSvdrrkpwapmktkqvqhrnhlqkscknankmvlwfeVDDTGCGIDPSKWDSVFESFEQ 713
Cdd:NF033092  508 GTITFR-----LLETHNRIIIS------------------------------------ISDQGLGIPKKDLDKIFDRFYR 546
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 18398532   714 ADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:NF033092  547 VDKARSRKMGGTGLGLAIAKEVVEAHGGRIWAESEEGKGT 586
PRK10490 PRK10490
sensor protein KdpD; Provisional
479-768 1.27e-17

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 88.94  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   479 RAELIRqLDARRraEASSNyksQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYAT-VTQIRKCSTALLRLLNNILD 557
Cdd:PRK10490  650 SEEQAR-LASER--EQLRN---ALLAALSHDLRTPLTVLFGQAEILTLDLASEGSPHARqASEIRQQVLNTTRLVNNLLD 723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   558 LSKVESGKlvleeaeFDLGRE---LEGLV----DMFSVQCINHNVEtvLDLSDDMPaLVRGDSARLVQIFANLISNSIKF 630
Cdd:PRK10490  724 MARIQSGG-------FNLRKEwltLEEVVgsalQMLEPGLSGHPIN--LSLPEPLT-LIHVDGPLFERVLINLLENAVKY 793
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   631 TTTGHII-LRGWCENiNSLHdemsvsvdrrkpwapmktkqvqhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFE 709
Cdd:PRK10490  794 AGAQAEIgIDAHVEG-ERLQ----------------------------------------LDVWDNGPGIPPGQEQLIFD 832
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532   710 SF-----EQADPsttrthgGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVD 768
Cdd:PRK10490  833 KFargnkESAIP-------GVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLETPPELE 889
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1047-1182 2.76e-17

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: 78.22  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1047 LLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSlnyksinaqapteehksFEEEtankvttretslrnssPYDLILM 1126
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALEL-----------------AREE----------------QPDLIIL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1127 DCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17574   48 DVMLPGMDGFEVCRRLRE----KGSDIPIIMLTAKDEEEDKVLGLELGADDYITKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1042-1192 3.21e-17

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: 85.79  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1042 EGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPY 1121
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLR---------------------------------EEPP 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:COG2204   48 DLVLLDLRMPGMDGLELLRELRALDP----DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAV 114
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
499-564 1.12e-16

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 75.30  E-value: 1.12e-16
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532     499 KSQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESG 564
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYLELL-LDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
494-743 1.93e-16

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 83.53  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   494 ASSNYKSQ-----FLANMSHELRTPMAAVIGLLDILisDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVL 568
Cdd:PRK10549  230 ASTLEKNEqmrrdFMADISHELRTPLAVLRGELEAI--QDGVRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGALAY 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   569 EEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDmpALVRGDSARLVQIFANLISNSIKFTTTGhiilrgwceniNSL 648
Cdd:PRK10549  308 RKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDS--ATVFGDPDRLMQLFNNLLENSLRYTDSG-----------GSL 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   649 HdemsVSVDRRkpwapmktkqvqhrnhlqkscknANKMVLWFEvdDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLG 728
Cdd:PRK10549  375 H----ISAEQR-----------------------DKTLRLTFA--DSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLG 425
                         250
                  ....*....|....*
gi 18398532   729 LCIVRNLVNKMGGEI 743
Cdd:PRK10549  426 LAICLNIVEAHNGRI 440
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
499-564 2.54e-16

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 74.17  E-value: 2.54e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532    499 KSQFLANMSHELRTPMAAVIGLLDILiSDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESG 564
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYLELL-RDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1045-1183 8.99e-16

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: 74.07  E-value: 8.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnssPyDLI 1124
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALA-----------EEEL---------------------P-DLI 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEiGTElHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:cd17538   48 LLDVMMPGMDGFEVCRRLKEDP-ETR-HIPVIMITALDDREDRIRGLEAGADDFLSKPI 104
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1046-1183 9.73e-16

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 74.08  E-value: 9.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAvdslnYKSINAQAPteehksfeeetankvttretslrnsspyDLIL 1125
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQA-----LQRAQAEPP----------------------------DLIL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1126 MDCQMPKMDGYEATKAIRrAEIGTElHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:cd19920   48 LDVMMPGMDGFEVCRRLK-ADPATR-HIPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
499-560 2.91e-15

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: 71.47  E-value: 2.91e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532  499 KSQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSK 560
Cdd:cd00082    4 KGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1047-1184 3.37e-15

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: 73.02  E-value: 3.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1047 LLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDslnyksinaQAPTEEhksfeeetankvttretslrnsspYDLILM 1126
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLE---------YALSGI------------------------YDLIIL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1127 DCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd17625   48 DIMLPGMDGLEVLKSLREEGIET----PVLLLTALDAVEDRVKGLDLGADDYLPKPFS 101
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1045-1184 3.70e-15

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: 73.22  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMG--ATVTAVWDGQQAVDSLNYKSINAQAPTeehksfeeetankvttretslrnssPyD 1122
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADAPR-------------------------P-D 54
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1123 LILMDCQMPKMDGYEATKAIRRAEigtEL-HIPIVALTAhamSSDE---AKCLEVGMDAYLTKPID 1184
Cdd:cd17557   55 LILLDLNMPRMDGFEVLREIKADP---DLrRIPVVVLTT---SDAEediERAYELGANSYIVKPVD 114
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1044-1188 3.97e-15

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: 72.82  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinAQAPTEehksfeeetankvttretslrnsspYDL 1123
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLL------ASAEHS-------------------------FQL 49
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1124 ILMDCQMPKMDGYEATKAIRraEIGTELHIP-IVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLM 1188
Cdd:cd19933   50 VLLDLCMPEMDGFEVALRIR--KLFGRRERPlIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1036-1183 4.75e-15

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 80.37  E-value: 4.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1036 KNQKSLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqaPTEehksfeeetankvttretsl 1115
Cdd:PRK11091  518 EDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFD--------PDE-------------------- 569
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  1116 rnsspYDLILMDCQMPKMDGYEATKAIRRAEIGTELHiPIVALTAHAMsSDEAKCLEVGMDAYLTKPI 1183
Cdd:PRK11091  570 -----YDLVLLDIQLPDMTGLDIARELRERYPREDLP-PLVALTANVL-KDKKEYLDAGMDDVLSKPL 630
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
480-759 2.17e-14

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 77.19  E-value: 2.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   480 AELIRQLDARRRAEASSNYKSQFLANMSHELRTPMAAVIGLLDILISDdcLSNEQYAT-VTQIRKCSTALLRLLNNILDL 558
Cdd:PRK11100  237 RELAQALESMRVKLEGKAYVEQYVQTLTHELKSPLAAIRGAAELLQED--PPPEDRARfTGNILTQSARLQQLIDRLLEL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   559 SKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDdmpALVRGDSARLVQIFANLISNSIKFTTTGhiil 638
Cdd:PRK11100  315 ARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRPDD---ARVLGDPFLLRQALGNLLDNAIDFSPEG---- 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   639 rgwceninslhDEMSVSVDRRkpwapmkTKQVQhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFESFEqadpST 718
Cdd:PRK11100  388 -----------GTITLSAEVD-------GEQVA------------------LSVEDQGPGIPDYALPRIFERFY----SL 427
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 18398532   719 TRTHGG---TGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:PRK11100  428 PRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTL 471
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
479-767 3.14e-14

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 77.80  E-value: 3.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   479 RAELIRQLDARRRAEASSNYKSqflaNMSHELRTPMAAVIGLLDIliSDDCLSNEQYAT--VTQIRKcSTALLRLL-NNI 555
Cdd:PRK13837  434 RDALERRLEHARRLEAVGTLAS----GIAHNFNNILGAILGYAEM--ALNKLARHSRAAryIDEIIS-AGARARLIiDQI 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   556 LDLSKVESGKLVleeaEFDLGRELEGLVDMFSVQcINHNVETVLDLsDDMPALVRGDSARLVQIFANLISNSIK-FTTTG 634
Cdd:PRK13837  507 LAFGRKGERNTK----PFDLSELVTEIAPLLRVS-LPPGVELDFDQ-DQEPAVVEGNPAELQQVLMNLCSNAAQaMDGAG 580
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   635 HIilrgwceninslhdemSVSVDRRKPWAPmktKQVQHRNhlqkscKNANKMVLwFEVDDTGCGIDPSKWDSVFESFeqa 714
Cdd:PRK13837  581 RV----------------DISLSRAKLRAP---KVLSHGV------LPPGRYVL-LRVSDTGAGIDEAVLPHIFEPF--- 631
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18398532   715 dpSTTRThGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTV 767
Cdd:PRK13837  632 --FTTRA-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPV 681
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
483-759 8.08e-14

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 75.45  E-value: 8.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   483 IRQLdarrraEASSNYKSQFLANMSHELRTPmaavigLLDILISDDCLSNEQYATVTQIRKcSTALL--------RLLNN 554
Cdd:NF040691  261 IRQL------EELSRLQQRFVSDVSHELRTP------LTTIRMAADVIHDSRDDFDPATAR-SAELLhteldrfeSLLSD 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   555 ILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLsDDMPALVRGDSARLVQIFANLISNSIKFTTTG 634
Cdd:NF040691  328 LLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDA-PGTPVVAEVDPRRVERVLRNLVVNAIEHGEGK 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   635 HIILRgwcenINSlhDEMSVSVdrrkpwapmktkqvqhrnhlqkscknankmvlwfEVDDTGCGIDPSKWDSVFESFEQA 714
Cdd:NF040691  407 PVVVT-----VAQ--DDTAVAV----------------------------------TVRDHGVGLKPGEVALVFDRFWRA 445
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 18398532   715 DPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:NF040691  446 DPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTL 490
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
483-753 1.68e-13

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 74.28  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   483 IRQLDARRRaeassnyksQFLANMSHELRTPMAAVIGLLDILISDDC---LSNEQYATVT-QIRKCSTallrLLNNILDL 558
Cdd:PRK11006  197 MHQLEGARR---------NFFANVSHELRTPLTVLQGYLEMMQDQPLegaLREKALHTMReQTQRMEG----LVKQLLTL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   559 SKVESGKLVLEEAEFD-------LGRELEGLVDMfsvqciNHNVETVLDlsddmPAL-VRGDSARLVQIFANLISNSIKF 630
Cdd:PRK11006  264 SKIEAAPTIDLNEKVDvpmmlrvLEREAQTLSQG------KHTITFEVD-----NSLkVFGNEDQLRSAISNLVYNAVNH 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   631 TTTG-HIILRgWceninslhdemsvsvdrrkpwapmktkqvqhrnhlQKSCKNAnkmvlWFEVDDTGCGIDPSKWDSVFE 709
Cdd:PRK11006  333 TPEGtHITVR-W-----------------------------------QRVPQGA-----EFSVEDNGPGIAPEHIPRLTE 371
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 18398532   710 SFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:PRK11006  372 RFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGT 415
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
499-745 4.23e-13

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 73.27  E-value: 4.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   499 KSQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQ----YATVTQIRKCStallRLLNNILDLSKVESGKLVLEEAEFD 574
Cdd:PRK09835  262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELedvlYSNLEELTRMA----KMVSDMLFLAQADNNQLIPEKKMLD 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   575 LGRELEGLVDMFSVQCINHNVETVLDlsdDMPALVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemsv 654
Cdd:PRK09835  338 LADEVGKVFDFFEAWAEERGVELRFV---GDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAI----------------- 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   655 svdrrkpwapmkTKQVQHRNHLQKSCknankmvlwfeVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRN 734
Cdd:PRK09835  398 ------------TVRCQEVDHQVQLV-----------VENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKS 454
                         250
                  ....*....|.
gi 18398532   735 LVNKMGGEIKV 745
Cdd:PRK09835  455 IVVAHKGTVAV 465
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1044-1192 5.59e-13

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: 66.67  E-value: 5.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGATVTA-VWDGQQAVdslnyksinaqAPTEEHKSfeeetankvttretslrnsspyD 1122
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAV-----------ELAKKHKP----------------------D 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1123 LILMDCQMPKMDGYEATKAIRRAEIGtelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd19932   48 LVIMDVKMPRLDGIEAAKIITSENIA-----PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1046-1184 5.94e-13

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: 66.35  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLIL 1125
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALA---------------------------------SGPYDLVI 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd17624   48 LDLGLPDGDGLDLLRRWRRQGQ----SLPVLILTARDGVDDRVAGLDAGADDYLVKPFA 102
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
457-759 6.38e-13

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: 72.21  E-value: 6.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  457 IFFIGCVCILILTNGVSKEMKLRAELIRqldarrrAEassnyK----SQFLANMSHELRTPMAAVIGLLDILISDDCL-- 530
Cdd:COG5806  167 IQLLAMLIAVYLIENLIENILLRKELQR-------AE-----KlevvSELAASIAHEVRNPLTVVRGFIQLLQEPELSde 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  531 SNEQYAtvtqirkcSTALLRL------LNNILDLSKVESGKLVleeaEFDLGRELEGLVDMFSVQCINHNVETVLDLSDd 604
Cdd:COG5806  235 KRKQYI--------RIALEELdraeaiITDYLTFAKPQPEKLE----KIDVSEELEHVIDVLSPYANMNNVEIQTELEP- 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  605 mPALVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceNINSLHDEMSVsvdrrkpwapmktkqvqhrnhlqkscknan 684
Cdd:COG5806  302 -GLYIEGDRQKLQQCLINIIKNGIEAMPNGGTL------TIDVSIDKNKV------------------------------ 344
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  685 kmvlWFEVDDTGCGIDPskwdsvfESFEQ-ADP--STTRThgGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:COG5806  345 ----IISIKDTGVGMTK-------EQLERlGEPyfSTKEK--GTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITL 409
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1043-1192 6.59e-13

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: 68.83  E-value: 6.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1043 GIRILLAEDTPVLQRVATIMLEKMGATVTAV-WDGQQAVdslnyksinaqAPTEEHKsfeeetankvttretslrnsspY 1121
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVAEaADGEDAV-----------ELVRELK----------------------P 49
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRaeigtELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:COG3707   50 DLVIVDIDMPDRDGLEAARQISE-----ERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1045-1182 8.10e-13

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: 65.57  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKM-GATV--TAVwDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnsspY 1121
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEaGFEVvgEAE-NGEEALELL-----------EEHK----------------------P 46
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:COG4753   47 DLVITDINMPGMDGLELLEAIRE----LDPDTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1044-1192 2.78e-12

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


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 64.74  E-value: 2.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWD-GQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnssPyD 1122
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVVGIADsGEEAIELA-----------EENK---------------------P-D 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532 1123 LILMDCQMP-KMDGYEATKAIRRaeigtELHIPIVALTAHamsSDEA---KCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17534   48 LILMDINLKgDMDGIEAAREIRE-----KFDIPVIFLTAY---SDEEtleRAKETNPYGYLVKPFNERELKAAI 113
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1046-1182 2.93e-12

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: 63.94  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSInaqapteehksfeeetankvttretslrnsspyDLIL 1125
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIP---------------------------------DLII 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRraEIGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd19927   48 SDIIMPGVDGYSLLGKLR--KNADFDTIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1041-1195 4.36e-12

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 64.61  E-value: 4.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1041 LEGIRILLAEDTPVLQRVATIMLEKMG--ATVTAVWDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrns 1118
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALL-----------AEHR-------------------- 49
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1119 spYDLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:COG4565   50 --PDLILLDIYLPDGDGLELLRELRARGP----DVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERY 120
PRK10604 PRK10604
sensor protein RstB; Provisional
499-745 4.88e-12

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 69.63  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   499 KSQFLANMSHELRTPMAAVIGLLDIliSDDCLSNEQYATVTQIrkcsTALLRLLNNILDLSKVESGKLVLEEAEFDLGRE 578
Cdd:PRK10604  212 KKQLIDGIAHELRTPLVRLRYRLEM--SDNLSAAESQALNRDI----GQLEALIEELLTYARLDRPQNELHLSEPDLPAW 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   579 LEGLVDmfSVQCINHNVETVLDLSDdMPALVRGDSARLVQIFANLISNSIKFTttghiilrgwceninslHDEMSVSVDR 658
Cdd:PRK10604  286 LSTHLA--DIQAVTPEKTVRLDTPH-QGDYGALDMRLMERVLDNLLNNALRYA-----------------HSRVRVSLLL 345
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   659 rkpwapmktkqvqhrnhlqksckNANKMVLwfEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNK 738
Cdd:PRK10604  346 -----------------------DGNQACL--IVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALA 400

                  ....*..
gi 18398532   739 MGGEIKV 745
Cdd:PRK10604  401 MGGSVNC 407
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
688-759 5.63e-12

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: 63.24  E-value: 5.63e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532  688 LWFEVDDTGCGIDPSKWDSVFESFEQADPSttRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16950   31 TRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIEL 100
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1120-1185 8.35e-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: 63.23  E-value: 8.35e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1120 PYDLILMDCQMPKMDGYEATKAIRRAEigTELHIPIVALTAHamsSDEA---KCLEVGMDAYLTKPIDR 1185
Cdd:cd17551   45 PPDLILLDYMMPGMDGLEFIRRLRALP--GLEDVPIVMITAD---TDREvrlRALEAGATDFLTKPFDP 108
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
688-759 9.90e-12

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: 62.82  E-value: 9.90e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532  688 LWFEVDDTGCGIDPSKWDSVFESFeqadpSTTRTHG-GTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16943   36 VLIEVEDTGSGIDPEILGRIFDPF-----FTTKPVGeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIIL 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1120-1192 1.03e-11

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: 62.91  E-value: 1.03e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532 1120 PYDLILMDCQMPKMDGYEATKAIRRAeigtELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17535   44 RPDVVLMDLSMPGMDGIEALRRLRRR----YPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1046-1192 1.25e-11

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: 62.73  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKSfeeetankvttretslrnsspyDLIL 1125
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML-----------AEHRP----------------------TLVI 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEigtEL-HIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17598   48 SDIVMPEMDGYELCRKIKSDP---DLkDIPVILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRI 112
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1046-1182 1.56e-11

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


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 62.40  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAvdsLNYKSINAQAPTEEHKsfeeetankvttretslrnssPYDLIL 1125
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEA---LNKLENLAKEGNDLSK---------------------ELDLII 56
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIGTElhIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd19924   57 TDIEMPKMDGYELTFELRDDPRLAN--IPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
612-743 1.79e-11

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: 62.10  E-value: 1.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  612 DSARLVQIFANLISNSIKFTTTGhiilrgwceniNSLHdemsvsvdrrkpwapMKTKQVQHrnhlqkscknankmVLWFE 691
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTG-----------GKLR---------------IRAAQTPQ--------------EVRLD 40
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18398532  692 VDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEI 743
Cdd:cd16946   41 VEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAICHNIALAHGGTI 92
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1047-1188 2.39e-11

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


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 61.91  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1047 LLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLILM 1126
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAK---------------------------------DEKPDLIIL 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532 1127 DCQMPKMDGYEATKAIRRAEIGTElhIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID-RKLM 1188
Cdd:cd19937   48 DLMLPGIDGLEVCRILRSDPKTSS--IPIIMLTAKGEEFDKVLGLELGADDYITKPFSpRELL 108
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1046-1182 2.55e-11

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: 61.30  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDslnyksinaQAPTEEhksfeeetankvttretslrnsspYDLIL 1125
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLH---------LALTNE------------------------YDLII 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd19935   48 LDVMLPGLDGLEVLRRLRAAGKQT----PVLMLTARDSVEDRVKGLDLGADDYLVKP 100
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
692-745 2.74e-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: 61.29  E-value: 2.74e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 18398532  692 VDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKV 745
Cdd:cd16939   35 VEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVALWHGGHVEC 88
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1096-1192 3.23e-11

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: 61.50  E-value: 3.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1096 EHKSFEEETANKVTTRETSLRNSSPyDLILMDCQMPKMDGYEATKAIRRAEIGTElhIPIVALTAHAMSSDEAKCLEVGM 1175
Cdd:cd17618   21 ERAGFDVVEAEDAESAVNLIVEPRP-DLILLDWMLPGGSGIQFIRRLKRDEMTRD--IPIIMLTARGEEEDKVRGLEAGA 97
                         90
                 ....*....|....*..
gi 18398532 1176 DAYLTKPIDRKLMVSTI 1192
Cdd:cd17618   98 DDYITKPFSPRELVARI 114
PRK09303 PRK09303
histidine kinase;
479-752 5.47e-11

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 65.74  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   479 RAELIRQLDArrraeassnyKSQFLANMSHELRTPM-AAVIGL--LDILISDDclSNEQYATVT-----QIRKCSTALLR 550
Cdd:PRK09303  141 NETLLEQLKF----------KDRVLAMLAHDLRTPLtAASLALetLELGQIDE--DTELKPALIeqlqdQARRQLEEIER 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   551 LLNNILDLSKVESGKLVLEEAEFDLGRELEGLVDMFSVQCINHNVETVLDLSDDMPaLVRGDSARLVQIFANLISNSIKF 630
Cdd:PRK09303  209 LITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLP-SVYADQERIRQVLLNLLDNAIKY 287
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   631 TTTGHIIlrgwceNINSLHdemsvsvdrrkpwapmKTKQ-VQhrnhlqkscknankmvlwFEVDDTGCGIDPSKWDSVFE 709
Cdd:PRK09303  288 TPEGGTI------TLSMLH----------------RTTQkVQ------------------VSICDTGPGIPEEEQERIFE 327
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 18398532   710 -SFE-QADPSTTrthgGTGLGLCIVRNLVNKMGGEIKVVQKNGLG 752
Cdd:PRK09303  328 dRVRlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQG 368
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
445-759 5.61e-11

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 66.92  E-value: 5.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   445 KTLIILISASVcIF-----FIGCVCILiltNGVSKEMKLRAELIRQldaRRRAEASsnyksQFLANMSHELRTPMAAVIG 519
Cdd:PRK11360  343 RTIELSVSTSL-LHnthgeMIGALVIF---SDLTERKRLQRRVARQ---ERLAALG-----ELVAGVAHEIRNPLTAIRG 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   520 LLDILISDDCLSNEQYATVTQIRKCsTALLRLLNNILDLSKVESGKLVleeaefdlGRELEGLVD--MFSVQCINH--NV 595
Cdd:PRK11360  411 YVQIWRQQTSDPPSQEYLSVVLREV-DRLNKVIDQLLEFSRPRESQWQ--------PVSLNALVEevLQLFQTAGVqaRV 481
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   596 ETVLDLSDDMPAlVRGDSARLVQIFANLISNSIK-FTTTGHIILRGWceninslhdemsvsvdrrkpwapmktkqvqhrn 674
Cdd:PRK11360  482 DFETELDNELPP-IWADPELLKQVLLNILINAVQaISARGKIRIRTW--------------------------------- 527
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   675 hlqkSCKNANKMVlwfEVDDTGCGIDPSKWDSVFESFeqadpSTTRTHGgTGLGLCIVRNLVNKMGGEIKVVQKNGLGTL 754
Cdd:PRK11360  528 ----QYSDGQVAV---SIEDNGCGIDPELLKKIFDPF-----FTTKAKG-TGLGLALSQRIINAHGGDIEVESEPGVGTT 594

                  ....*
gi 18398532   755 MRLYL 759
Cdd:PRK11360  595 FTLYL 599
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
612-759 6.44e-11

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: 60.58  E-value: 6.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  612 DSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemsvsvdrrkpwapmktkqvqhRNHLQKSCKNANKMVlwfe 691
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGRI-----------------------------------RCILEKFRLNRFLLT---- 41
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  692 VDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16925   42 VSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1045-1184 7.95e-11

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: 60.64  E-value: 7.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGA--TVTAVwDGQQAVdslnyksinAQAPTEehksfeeetankvttretslrnssPYD 1122
Cdd:cd17552    3 RILVIDDEEDIREVVQACLEKLAGweVLTAS-SGQEGL---------EKAATE------------------------QPD 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532 1123 LILMDCQMPKMDGYEATKAIRrAEIGTElHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd17552   49 AILLDVMMPDMDGLATLKKLQ-ANPETQ-SIPVILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
504-750 1.49e-10

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


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 64.25  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   504 ANMSHELRTPMAAVIGLL-----DILISDDCLSNEQYATVTQirkcstaLLRLLNNILDLSKVESGKLVLEEAEFDLGRE 578
Cdd:NF012226  143 AAIAHELRTPITILQGRLqgildGVFEPDPALFKSLLNQVEG-------LSHLVEDLRTLSLVENQQLRLNYESVDLKDS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   579 LEGLVDMFSVQCINHNVETVLDLSDDmpaLVRGDSARLVQIFANLISNSIKFTTTGHIILRgwceninslhdemsvsvdr 658
Cdd:NF012226  216 IEKVLKMFEDRLEQAQLTIVLNLTAT---PVFCDRRRIEQVLIALIDNAIRYANAGKLKIS------------------- 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   659 rkpwapmktkqvqhrnhlqkSCKNANKMVLWFEvdDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNK 738
Cdd:NF012226  274 --------------------SSVIQDDWILQIE--DEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIA 331
                         250
                  ....*....|..
gi 18398532   739 MGGEIKVVQKNG 750
Cdd:NF012226  332 HKGSIEYSNSQG 343
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1122-1182 1.95e-10

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: 59.32  E-value: 1.95e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17627   44 DAVVLDVMMPRLDGLEVCRRLRAAGN----DLPILVLTARDSVSDRVAGLDAGADDYLVKP 100
pleD PRK09581
response regulator PleD; Reviewed
1122-1197 2.03e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 64.54  E-value: 2.03e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRrAEIGTElHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTK 1197
Cdd:PRK09581   48 DIILLDVMMPGMDGFEVCRRLK-SDPATT-HIPVVMVTALDDPEDRVRGLEAGADDFLTKPINDVALFARVKSLTR 121
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
616-753 3.91e-10

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: 58.11  E-value: 3.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  616 LVQIFANLISNSIKFTTtghiilrgwceninslhdemsvsvDRRKPWApmktkQVQHRnhlqkscKNANKMVlwFEVDDT 695
Cdd:cd16921    1 LGQVLTNLLGNAIKFRR------------------------PRRPPRI-----EVGAE-------DVGEEWT--FYVRDN 42
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  696 GCGIDPSKWDSVFESFEQADPSTTrtHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:cd16921   43 GIGIDPEYAEKVFGIFQRLHSREE--YEGTGVGLAIVRKIIERHGGRIWLESEPGEGT 98
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1044-1182 4.12e-10

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: 58.56  E-value: 4.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGA-TV--TAVwDGQQAVDSlnyksINAQAPteehksfeeetankvttretslrnssp 1120
Cdd:cd17541    1 IRVLIVDDSAVMRKLLSRILESDPDiEVvgTAR-DGEEALEK-----IKELKP--------------------------- 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532 1121 yDLILMDCQMPKMDGYEATKAIRRaeigteLH-IPIVALTAHAMSSDEA--KCLEVGMDAYLTKP 1182
Cdd:cd17541   48 -DVITLDIEMPVMDGLEALRRIMA------ERpTPVVMVSSLTEEGAEItlEALELGAVDFIAKP 105
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1121-1192 4.80e-10

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: 58.19  E-value: 4.80e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532 1121 YDLILMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17616   43 YDIILLDLNLPDMSGYEVLRTLRLAKVKT----PILILSGLADIEDKVKGLGFGADDYMTKPFHKDELVARI 110
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1045-1193 5.15e-10

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: 58.16  E-value: 5.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehksfeeetankvttreTSLRNSSPyDLI 1124
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVL--------------------------------PYVRHTPP-DLI 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID-RKLM--VSTIL 1193
Cdd:cd19938   48 LLDLMLPGTDGLTLCREIRRFS-----DVPIIMVTARVEEIDRLLGLELGADDYICKPYSpREVVarVKAIL 114
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
690-759 6.18e-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: 57.68  E-value: 6.18e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  690 FEVDDTGCGIDPSKWDSVFESfeqadPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16915   39 IEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRI 103
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1045-1195 7.20e-10

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: 57.77  E-value: 7.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRII---------------------------------DEQPSLV 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRaeigtELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:cd19939   48 VLDIMLPGMDGLTVCREVRE-----HSHVPILMLTARTEEMDRVLGLEMGADDYLCKPFSPRELLARVRAL 113
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
589-759 7.57e-10

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 62.56  E-value: 7.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  589 QCINHNVETVLDLSDDMPALVRGDSArLVQIFANLISNSIKftttgHiilrgwCENINSLHDEMSVSVDRRKPWapmktk 668
Cdd:COG3290  256 RARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIE-----A------VEKLPEEERRVELSIRDDGDE------ 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  669 qvqhrnhlqkscknankmvLWFEVDDTGCGIDPSKWDSVFES-FeqadpsTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQ 747
Cdd:COG3290  318 -------------------LVIEVEDSGPGIPEELLEKIFERgF------STKLGEGRGLGLALVKQIVEKYGGTIEVES 372
                        170
                 ....*....|..
gi 18398532  748 KNGLGTLMRLYL 759
Cdd:COG3290  373 EEGEGTVFTVRL 384
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
501-762 8.36e-10

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: 62.83  E-value: 8.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  501 QFLANMSHELRTPMAAVIGLLDIL-ISDDClsNEQYATV--TQIRKCSTALLRLLNnildLSKVESGKLVLEeaefDLGR 577
Cdd:COG5805  289 QLAAGIAHEIRNPLTSIKGFLQLLqPGIED--KEEYFDImlSELDRIESIISEFLA----LAKPQAVNKEKE----NINE 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  578 ELEGLVDMFSVQCINHNVETVLDLSDDMPALVrGDSARLVQIFANLISNSIKFTTTGHIIlrgwceninSLHdemsvsvd 657
Cdd:COG5805  359 LIQDVVTLLETEAILHNIQIRLELLDEDPFIY-CDENQIKQVFINLIKNAIEAMPNGGTI---------TIH-------- 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  658 rrkpwapmkTKQVQHRNHLqkscknankmvlwfEVDDTGCGIDPSKWDSVFESFeqadpSTTRTHGgTGLGLCIVRNLVN 737
Cdd:COG5805  421 ---------TEEEDNSVII--------------RVIDEGIGIPEERLKKLGEPF-----FTTKEKG-TGLGLMVSYKIIE 471
                        250       260
                 ....*....|....*....|....*
gi 18398532  738 KMGGEIKVVQKNGLGTLMRLYLILS 762
Cdd:COG5805  472 NHNGTIDIDSKVGKGTTFTITLPLS 496
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1046-1192 1.12e-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: 56.93  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLIL 1125
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALL---------------------------------EGSPDLVV 47
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRaeigtELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17623   48 LDVMLPKMNGLDVLKELRK-----TSQVPVLMLTARGDDIDRILGLELGADDYLPKPFNPRELVARI 109
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1043-1184 1.30e-09

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: 57.11  E-value: 1.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1043 GIRILLAEdtpvlqrvatiMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnsspYD 1122
Cdd:COG5803   13 GIRMLLKE-----------VLKKEGYEVFQAANGKEALEKV-----------KELK----------------------PD 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532 1123 LILMDCQMPKMDGYEATKAIRraEIGTElhIPIVALTAHAMSS--DEAKCLevGMDAYLTKPID 1184
Cdd:COG5803   49 LVLLDMKMPGMDGIEILKEIK--EIDPD--IPVIMMTAYGELDmvEEAKEL--GAKGYFTKPFD 106
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1045-1192 1.41e-09

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: 56.71  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqapteehksfeeetankvttretslRNSSPyDLI 1124
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAF--------------------------------REVRP-DLV 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1125 LMDCQMPKMDGYEATKAIRraeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17626   49 LLDLMLPGIDGIEVCRQIR-----AESGVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELVARI 111
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
604-748 1.58e-09

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: 57.14  E-value: 1.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  604 DMPALVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceNINSLHDEMSVSVDrrkpwapmktkqvqhrnhlqksckna 683
Cdd:cd16947    9 DRPIYANANTEALQRILKNLISNAIKYGSDGKFL------GMTLREDEKHVYID-------------------------- 56
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  684 nkmvlwfeVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQK 748
Cdd:cd16947   57 --------IWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSK 113
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
620-753 1.69e-09

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: 56.44  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  620 FANLISNSIKFT-TTGHIILRGWceninslhdemsvsvdrrkpwapmktkQVQHRNHlqkscknankmvlwFEVDDTGCG 698
Cdd:cd16952    5 FSNLVSNAVKYTpPSDTITVRWS---------------------------QEESGAR--------------LSVEDTGPG 43
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  699 IDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGT 753
Cdd:cd16952   44 IPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGS 98
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
690-759 2.84e-09

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: 55.85  E-value: 2.84e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532  690 FEVDDTGCGIDPSKWDSVFESFeqadpSTTRTHG-GTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16919   50 LEVSDTGSGMPAEVLRRAFEPF-----FTTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYL 115
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
496-745 3.12e-09

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: 61.30  E-value: 3.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    496 SNYkSQFLANMS----HELRTPMAAVIGLLDILISDDcLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESGKLVLEEA 571
Cdd:TIGR03785  479 RQY-THYLENMSsrlsHELRTPVAVVRSSLENLELQA-LEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVE 556
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    572 EFDLGRELEGLvdMFSVQCINHNVETVLDLSDDmPALVRGDSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdE 651
Cdd:TIGR03785  557 DFDLSEVLSGC--MQGYQMTYPPQRFELNIPET-PLVMRGSPELIAQMLDKLVDNAREFSPEDGLI-------------E 620
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532    652 MSVSvdrrkpwapmktkqvQHRNHlqkscknankmvLWFEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCI 731
Cdd:TIGR03785  621 VGLS---------------QNKSH------------ALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLGLGLYI 673
                          250
                   ....*....|....
gi 18398532    732 VRNLVNKMGGEIKV 745
Cdd:TIGR03785  674 VRLIADFHQGRIQA 687
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1046-1182 3.20e-09

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: 55.89  E-value: 3.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehKSFEEETAnkvttretslrnsspyDLIL 1125
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREAL-----------------EKVEEEQP----------------DLIL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17614   48 LDLMLPEKDGLEVCREVRKTS-----NVPIIMLTAKDSEVDKVLGLELGADDYVTKP 99
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1046-1182 3.94e-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: 55.75  E-value: 3.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDslnyksinaQAPTEehksfeeetankvttretslrnssPYDLIL 1125
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALF---------QGEEE------------------------PYDLVV 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd19934   48 LDLGLPGMDGLSVLRRWRSEGRAT----PVLILTARDSWQDKVEGLDAGADDYLTKP 100
envZ PRK09467
osmolarity sensor protein; Provisional
684-763 7.18e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 59.54  E-value: 7.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   684 NKMVLWFEVDDTGCGIDPSKWDSVFESFEQADpsTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILST 763
Cdd:PRK09467  358 EGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPLTT 435
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1045-1199 8.55e-09

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 57.51  E-value: 8.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnsSPYDLI 1124
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD----------------------------------DSIDLL 48
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1125 LMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTKPS 1199
Cdd:PRK10955   49 LLDVMMPKKNGIDTLKELRQTH-----QTPVIMLTARGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRRS 118
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
690-759 1.09e-08

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: 53.87  E-value: 1.09e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  690 FEVDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16949   33 ITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWL 102
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1044-1192 1.24e-08

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: 54.21  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGATV--TAVwDGQQAVDSlnYKsinaqapteEHKSfeeetankvttretslrnsspy 1121
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVvgEAA-NGEEAVEK--YK---------ELKP---------------------- 46
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRraEIGTELHipIVALTahAMSSDEA--KCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17542   47 DLVTMDITMPEMDGIEALKEIK--KIDPNAK--VIMCS--AMGQEEMvkEAIKAGAKDFIVKPFQPERVLEAV 113
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
504-759 2.33e-08

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 57.87  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   504 ANMSHELRTPMAAVIGLLDILISDDCLSNEQYATVTQIRKCSTALLRLLNNILDLSKVESgklvLEEAEFDLGRELEGLV 583
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTH----LALQAVDLNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   584 DMFSVQCINHNVETVLDLSDDMPALvRGDSARLVQIFANLISNSIkftttgHIILRgwceninslHDEMSVSVDRRKpwa 663
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPEI-QADPDRLTQVLLNLYLNAI------QAIGQ---------HGVISVTASESG--- 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   664 pmktKQVQHRnhlqkscknankmvlwfeVDDTGCGIDPSKWDSVFesfeqaDPSTTRTHGGTGLGLCIVRNLVNKMGGEI 743
Cdd:PRK10364  379 ----AGVKIS------------------VTDSGKGIAADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTI 430
                         250
                  ....*....|....*.
gi 18398532   744 KVVQKNGLGTLMRLYL 759
Cdd:PRK10364  431 QVASQEGKGATFTLWL 446
PRK15479 PRK15479
transcriptional regulator TctD;
1044-1203 4.36e-08

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 55.11  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAvdslnyksinaqapteEHksfeeetankvttretsLRNSSPYDL 1123
Cdd:PRK15479    1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAA----------------DH-----------------LLQSEMYAL 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1124 ILMDCQMPKMDGYEATKAIRRAeiGTELhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTKPSAFQT 1203
Cdd:PRK15479   48 AVLDINMPGMDGLEVLQRLRKR--GQTL--PVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQV 123
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1050-1182 4.88e-08

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: 51.99  E-value: 4.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1050 EDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehksfeeetankvttreTSLRNSSPyDLILMDCQ 1129
Cdd:cd17602    5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRAL--------------------------------TTLLNSKP-DLILIDID 51
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18398532 1130 MPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17602   52 MPDLDGYELCSLLRKSSALK--DTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
ompR PRK09468
osmolarity response regulator; Provisional
1042-1188 5.91e-08

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 54.98  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1042 EGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAvdslnyksinaqapteehksfeeetaNKVTTRETslrnsspY 1121
Cdd:PRK09468    4 ENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQM--------------------------DRLLTRES-------F 50
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID-RKLM 1188
Cdd:PRK09468   51 HLMVLDLMLPGEDGLSICRRLRSQNN----PTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFNpRELL 114
PRK15115 PRK15115
response regulator GlrR; Provisional
1045-1200 7.04e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 56.38  E-value: 7.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSInaqapteehksfeeetankvttretslrnsspyDLI 1124
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKV---------------------------------DLV 53
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  1125 LMDCQMPKMDGYEATKAIRRAEIGtelhIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI---LSLTKPSA 1200
Cdd:PRK15115   54 ISDLRMDEMDGMQLFAEIQKVQPG----MPVIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIddaLEQSAPAT 128
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1121-1184 7.22e-08

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: 51.86  E-value: 7.22e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532 1121 YDLILMDCQMPKMDGYEATKAIRraeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd17584   45 FDLVITDVHMPDMDGFEFLELIR-----LEMDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVS 103
orf27 CHL00148
Ycf27; Reviewed
1122-1197 7.22e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 54.72  E-value: 7.22e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRRaeigtELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTK 1197
Cdd:CHL00148   52 DLVILDVMMPKLDGYGVCQEIRK-----ESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVLR 122
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1045-1197 9.67e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 54.34  E-value: 9.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnsSPY-DL 1123
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLN----------------------------------EPWpDL 49
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532  1124 ILMDCQMPKMDGYEATKAIRRAEIGTElhIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTK 1197
Cdd:PRK10161   50 ILLDWMLPGGSGIQFIKHLKRESMTRD--IPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1045-1192 9.68e-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: 51.53  E-value: 9.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQ---------------------------------SKKFDLI 48
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1125 LMDCQMPKMDGYEATKAIRR--AEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17562   49 ITDQNMPNMDGIELIKELRKlpAYKFT----PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1045-1182 1.16e-07

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: 51.58  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDslnyksinaqapteehksfeeetankvTTRETSlrnssPyDLI 1124
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALA---------------------------AAREFR-----P-DAV 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17615   48 VLDIMLPDMDGLEVLRRLRADGPDV----PVLFLTAKDSVEDRIAGLTAGGDDYVTKP 101
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1045-1195 1.18e-07

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 55.62  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinAQAPTeehksfeeetankvttretslrnsspyDLI 1124
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLF------ADIHP---------------------------DVV 52
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532  1125 LMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPID---RKLMVSTILSL 1195
Cdd:PRK11361   53 LMDIRMPEMDGIKALKEMRSHETRT----PVILMTAYAEVETAVEALRCGAFDYVIKPFDldeLNLIVQRALQL 122
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1045-1195 1.54e-07

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: 51.23  E-value: 1.54e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqapteehksfeeetankvttretslRNSSPyDLI 1124
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVI--------------------------------AREKP-DAV 48
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGtelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSL 1195
Cdd:cd17622   49 LLDIMLPGIDGLTLCRDLRPKYQG-----PILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRAL 114
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1046-1183 1.59e-07

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 51.21  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSINAQAPTEEHKsfeeetankvttretslrnsspYDLIL 1125
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSNFNEPK----------------------VNMII 58
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532 1126 MDCQMPKMDGYEATKAIRraEIGTELHIPIValtahAMSSDE-----AKCLEVGMDAYLTKPI 1183
Cdd:cd17581   59 TDYCMPGMTGYDLLKKVK--ESSALKEIPVV-----IMSSENiptriSRCLEEGAEDFLLKPV 114
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1045-1189 1.60e-07

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: 50.85  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSInaqapteehksfeeetankvttretslrnsspyDLI 1124
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI---------------------------------DLV 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID-RKLMV 1189
Cdd:cd17619   49 LLDINLPGKDGLSLTRELREQS-----EVGIILVTGRDDEVDRIVGLEIGADDYVTKPFNpRELLV 109
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
472-773 1.64e-07

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 55.71  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   472 VSKEMKL-RAELIRQLDARRraeassnyksQFLANMSHELRTPMAAVIGLLDILISDDCLSNEQyATVTQIRKCSTALLR 550
Cdd:PRK10618  432 VNKKLQQaQREYEKNQQARK----------AFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQ-PELDQLAEQSDVLVR 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   551 LLNNILDLSKVESGKLVLEEAEFDLGRELEGLV-DMFSV------QCINHNvetVLDLSDdmpaLVRGDSARLVQIFANL 623
Cdd:PRK10618  501 LVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLpEVLPAikrkglQLLIHN---HLKAEQ----LRIGDRDALRKILLLL 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   624 ISNSIKFTTTGHIilrgwceninslhdemSVSVDRRKpwapmktkqvQHRNHLQkscknankmvlwFEVDDTGCGIDPSK 703
Cdd:PRK10618  574 LNYAITTTAYGKI----------------TLEVDQDE----------SSPDRLT------------IRILDTGAGVSIKE 615
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   704 WDSVFESFeQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYLILSTPDTVDQNIQP 773
Cdd:PRK10618  616 LDNLHFPF-LNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAADPEVEEEEE 684
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
616-759 2.29e-07

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: 50.48  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  616 LVQIFANLISNSIKFT--TTGHIILRgwceninslhdemsVSVDRrkpwapmktkQVQHRNHLQKscknankMVLWFEVD 693
Cdd:cd16918    1 LIQVFLNLVRNAAQALagSGGEIILR--------------TRTQR----------QVTLGHPRHR-------LALRVSVI 49
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532  694 DTGCGIDPSKWDSVFesfeqaDPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGlGTLMRLYL 759
Cdd:cd16918   50 DNGPGIPPDLQDTIF------YPMVSGRENGTGLGLAIAQNIVSQHGGVIECDSQPG-HTVFSVSL 108
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1046-1192 2.67e-07

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: 50.66  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLIL 1125
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLS---------------------------------DQPPDVVL 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAmSSDEAkclevgMDA-------YLTKPIDRKLMVSTI 1192
Cdd:cd17572   48 LDLKLPDMSGMEILKWIQERSLPT----SVIVITAHG-SVDIA------VEAmrlgaydFLEKPFDADRLRVTV 110
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1046-1182 2.92e-07

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: 49.86  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehksfeeetankvttRETSLRNssPyDLIL 1125
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGL------------------------------LEAATRK--P-DLII 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRraEIGTelhIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17620   48 LDLGLPDMDGLEVIRRLR--EWSA---VPVIVLSARDEESDKIAALDAGADDYLTKP 99
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1122-1192 3.29e-07

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: 49.97  E-value: 3.29e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRraeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd18159   44 DLVLLDINLPYFDGFYWCREIR-----QISNVPIIFISSRDDNMDQVMAINMGGDDYITKPFDLDVLLAKI 109
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1045-1183 6.49e-07

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: 49.12  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSlnyksinaqapteehksFEEETAnkvttretslrnsspyDLI 1124
Cdd:cd17555    2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLEL-----------------FRSEQP----------------DLV 48
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1125 LMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:cd17555   49 LCDLRMPEMDGLEVLKQITKESPDT----PVIVVSGAGVMSDAVEALRLGAWDYLTKPI 103
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1096-1182 8.88e-07

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 48.21  E-value: 8.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1096 EHKSFEEETankVTTRETSLR--NSSPYDLILMDCQMPKMDGYEATKAIRraeigTELHIPIVALTAHAMSSDEAKCLEV 1173
Cdd:cd19936   19 EAEGFSVET---YTDGASALDglNARPPDLAILDIKMPRMDGMELLQRLR-----QKSTLPVIFLTSKDDEIDEVFGLRM 90

                 ....*....
gi 18398532 1174 GMDAYLTKP 1182
Cdd:cd19936   91 GADDYITKP 99
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1121-1182 8.89e-07

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: 48.87  E-value: 8.89e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532 1121 YDLILMDCQMPKMDGYEATKAIRRAEigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd19923   46 FDFVITDWNMPNMDGLELLKTIRADG--ALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKP 105
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1122-1197 9.18e-07

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: 48.87  E-value: 9.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHamssDE---AK-CLEVGMDAYLTKPIDRKLMVSTILSLTK 1197
Cdd:cd17536   47 DIVITDIRMPGMDGLELIEKIRE----LYPDIKIIILSGY----DDfeyAQkAIRLGVVDYLLKPVDEEELEEALEKAKE 118
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1119-1193 1.06e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 51.22  E-value: 1.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  1119 SPYDLILMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVS---TIL 1193
Cdd:PRK10710   53 TPPDLILLDLMLPGTDGLTLCREIRRFS-----DIPIVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVArvkTIL 125
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
609-757 1.20e-06

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: 48.56  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  609 VRGDSARLVQIFANLISNSIKFTTTGHIilrgwceninslhdemsVSVdrrkpwapmktkQVQHRNHLQkscknankmvl 688
Cdd:cd16940    7 VQGDALLLFLLLRNLVDNAVRYSPQGSR-----------------VEI------------KLSADDGAV----------- 46
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532  689 wFEVDDTGCGIDPSKWDSVFESFEQADPSTTrthGGTGLGLCIVRNLVNKMGGEIKV--VQKNGLGTLMRL 757
Cdd:cd16940   47 -IRVEDNGPGIDEEELEALFERFYRSDGQNY---GGSGLGLSIVKRIVELHGGQIFLgnAQGGGLEAWVRL 113
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1046-1182 1.44e-06

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: 47.78  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSINAqapteehksfeeetankvttretslrnsspyDLIL 1125
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEI-------------------------------DLIL 49
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17582   50 TEVDLPVSSGFKLLSYIMRHKICK--NIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
PRK11517 PRK11517
DNA-binding response regulator HprR;
1044-1182 1.46e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 50.67  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteeHKSFEEEtankvttretslrnsspYDL 1123
Cdd:PRK11517    1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGL----------------YLALKDD-----------------YAL 47
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  1124 ILMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK11517   48 IILDIMLPGMDGWQILQTLRTAK-----QTPVICLTARDSVDDRVRGLDSGANDYLVKP 101
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1046-1182 1.51e-06

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 47.58  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslRNSSpyDLIL 1125
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFD-------------------------------RAGA--DIVL 47
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17621   48 LDLMLPGLSGTEVCRQLRARS-----NVPVIMVTAKDSEIDKVVGLELGADDYVTKP 99
PRK09483 PRK09483
response regulator; Provisional
1116-1192 2.49e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 49.72  E-value: 2.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18398532  1116 RNSSPyDLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:PRK09483   44 RTNAV-DVVLMDMNMPGIGGLEATRKILRYTP----DVKIIMLTVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAI 115
PRK13557 PRK13557
histidine kinase; Provisional
692-758 4.60e-06

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 50.82  E-value: 4.60e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532   692 VDDTGCGIDPSKWDSVFESFeqadpSTTRTHG-GTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLY 758
Cdd:PRK13557  329 VTDTGSGMPPEILARVMDPF-----FTTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLY 391
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
691-759 4.88e-06

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: 46.24  E-value: 4.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  691 EVDDTGCGIDPSKWDSVFesfeqaDPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16920   41 SVKDTGPGIAEEVAGQLF------DPFYTTKSEGLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTL 103
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
605-759 5.02e-06

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: 47.07  E-value: 5.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  605 MPALVRGDSARLVQIFANLISNSIKFT-TTGHIILRGWCENINSLHDEMSVSVDRRKpwapMKTKQVQHRnhlqksckna 683
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRnGGGNITFRVFLEGGSEDRSDRDWGPWRPS----MSDESVEIR---------- 66
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18398532  684 nkmvlwFEVDDTGCGIDPSKWDSVFESFEQADPSTTRthgGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16938   67 ------FEVEINDSGSPSIESASMRNSLNRRYNLSEL---GEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
692-754 5.27e-06

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 50.32  E-value: 5.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532   692 VDDTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKvVQKNGLGTL 754
Cdd:PRK09470  388 VDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVK-AEDSPLGGL 449
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1032-1183 5.52e-06

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 50.89  E-value: 5.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1032 ALDGKNQKSL---EGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehksfeeetaNKV 1108
Cdd:PRK09959  944 TVEAKAEQPItlpEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQAL-------------------------HKV 998
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1109 TTREtslrnsspYDLILMDCQMPKMDGYEATKAIRRAEIGtelhIPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:PRK09959  999 SMQH--------YDLLITDVNMPNMDGFELTRKLREQNSS----LPIWGLTANAQANEREKGLSCGMNLCLFKPL 1061
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1115-1182 8.27e-06

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 48.38  E-value: 8.27e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  1115 LRNSSPYDLILMDCQMPKMDGYEATKAIRRAEIGtelhIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK09836   39 LAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKG----MPILLLTALGTIEHRVKGLELGADDYLVKP 102
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
612-759 1.07e-05

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: 45.74  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  612 DSARLVQIFANLISNSIKFTTTGHIIlrgwceNINSLHDEMSVsvdrrkpwapmktkqvqhrnhlqkscknankmvlWFE 691
Cdd:cd16948    2 DAKWLSFIIGQIVSNALKYSKQGGKI------EIYSETNEQGV----------------------------------VLS 41
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18398532  692 VDDTGCGIDPSKWDSVFesfeqaDPSTTRTHG-----GTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16948   42 IKDFGIGIPEEDLPRVF------DKGFTGENGrnfqeSTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITF 108
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1044-1182 1.47e-05

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: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKSFEeetankvttretslrnsspydL 1123
Cdd:cd17544    1 IKVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVL-----------EQHPDIK---------------------L 48
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1124 ILMDCQMPKMDGYEATKAIRRAEIGTELhiPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:cd17544   49 VITDYNMPEMDGFELVREIRKKYSRDQL--AIIGISASGDNALSARFIKAGANDFLTKP 105
PRK10643 PRK10643
two-component system response regulator PmrA;
1109-1182 1.94e-05

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 47.34  E-value: 1.94e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532  1109 TTRE-TSLRNSSPYDLILMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK10643   32 TAREaEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTL----PVLILTARDTLEDRVAGLDVGADDYLVKP 102
PRK10610 PRK10610
chemotaxis protein CheY;
1044-1182 2.16e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 45.35  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGatVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretSLRnSSPYDL 1123
Cdd:PRK10610    6 LKFLVVDDFSTMRRIVRNLLKELG--FNNVEEAEDGVDALN-----------------------------KLQ-AGGFGF 53
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  1124 ILMDCQMPKMDGYEATKAIRraEIGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK10610   54 VISDWNMPNMDGLELLKTIR--ADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKP 110
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1117-1195 2.27e-05

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: 44.84  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1117 NSSPYDLILMDCQMPKMDGYEATKAIRRAEIGTELhipIValtahaMSSD---EAK--CLEVGMDAYLTKPIDRKLMVST 1191
Cdd:cd17593   42 REGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKV---IV------VSGDvqpEAKerVLELGALAFLKKPFDPEKLAQL 112

                 ....
gi 18398532 1192 ILSL 1195
Cdd:cd17593  113 LEEL 116
PRK10336 PRK10336
two-component system response regulator QseB;
1044-1204 2.59e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 46.81  E-value: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDL 1123
Cdd:PRK10336    1 MRILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALY---------------------------------SAPYDA 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1124 ILMDCQMPKMDGYEATKAIRraEIGTelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTILSLTKPSAFQT 1203
Cdd:PRK10336   48 VILDLTLPGMDGRDILREWR--EKGQ--REPVLILTARDALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRTNGQA 123

                  .
gi 18398532  1204 S 1204
Cdd:PRK10336  124 S 124
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1118-1192 3.61e-05

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: 44.13  E-value: 3.61e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532 1118 SSPYDLILMDCQMPKMDGYEATKAIRraEIGTELhiPIVALTAHAMSSDEAKCLevGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17554   42 SEDPDLVILDIKMPGMDGLETLRKIR--EKKPDL--PVIICTAYSEYKSDFSSW--AADAYVVKSSDLTELKETI 110
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1045-1200 7.15e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 45.72  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1045 RILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNyksinaqapteehksfeeetankvttretslrnSSPYDLI 1124
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLR---------------------------------QQPPDLV 51
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  1125 LMDCQMPKMDGYEATKAIRRAEigTELhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPID-RKLM--VSTILSLTKPSA 1200
Cdd:PRK11083   52 ILDVGLPDISGFELCRQLLAFH--PAL--PVIFLTARSDEVDRLVGLEIGADDYVAKPFSpREVAarVRTILRRVKKFA 126
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
616-743 8.57e-05

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: 42.94  E-value: 8.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  616 LVQIFANLISNSIKFT--TTGHIILRgwceninslhdemsvsvdrRKPWAPMKTkqvqhrnhlqkscknankmvlwFEVD 693
Cdd:cd16953    1 LGQVLRNLIGNAISFSppDTGRITVS-------------------AMPTGKMVT----------------------ISVE 39
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 18398532  694 DTGCGIDPSKWDSVFESFEQADPSTTRTHGGTGLGLCIVRNLVNKMGGEI 743
Cdd:cd16953   40 DEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSISRQIIEAHGGIS 89
PRK10766 PRK10766
two-component system response regulator TorR;
1103-1189 8.74e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 45.41  E-value: 8.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1103 ETANKVTTRETSLRNssPYDLILMDCQMPKMDGYEATKAIR-RAEIGtelhipIVALTAHAMSSDEAKCLEVGMDAYLTK 1181
Cdd:PRK10766   31 EAASGAGMREIMQNQ--HVDLILLDINLPGEDGLMLTRELRsRSTVG------IILVTGRTDSIDRIVGLEMGADDYVTK 102

                  ....*....
gi 18398532  1182 PID-RKLMV 1189
Cdd:PRK10766  103 PLElRELLV 111
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1122-1192 9.51e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 9.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRRAEIGTElhipIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:PRK10651   54 DLILLDLNMPGMNGLETLDKLREKSLSGR----IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
PLN03029 PLN03029
type-a response regulator protein; Provisional
1046-1183 9.60e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 45.02  E-value: 9.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYK---SINAQAPTEEHKSFEEETANkvttretslrnsspyd 1122
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHeddRSNPDTPSVSPNSHQEVEVN---------------- 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532  1123 LILMDCQMPKMDGYEATKAIRraEIGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:PLN03029   75 LIITDYCMPGMTGYDLLKKIK--ESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPV 133
glnL PRK11073
nitrogen regulation protein NR(II);
483-746 1.14e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 45.84  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   483 IRQLDARRRAEASSNYKSQFLA------NMSHELRTPMAAVIG---LLDILISDDCLSneQYatvTQIRKCSTALLRLLN 553
Cdd:PRK11073  108 MAPMDNQRRLSQEQLQHAQQVAardlvrGLAHEIKNPLGGLRGaaqLLSKALPDPALT--EY---TKVIIEQADRLRNLV 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   554 NILdLSKVESGKLVLEeaefDLGRELEGLVDMFSVQCiNHNVETVLDLSDDMPALVRgDSARLVQIFANLISNSIKF--T 631
Cdd:PRK11073  183 DRL-LGPQRPGTHVTE----SIHKVAERVVQLVSLEL-PDNVRLIRDYDPSLPELAH-DPDQIEQVLLNIVRNALQAlgP 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532   632 TTGHIILRgwceninslhdemsvsvdrrkpwapmkTKQVQHRNHLQKSCKNANKMvlwfEVDDTGCGIDPSKWDSVFEsf 711
Cdd:PRK11073  256 EGGTITLR---------------------------TRTAFQLTLHGERYRLAARI----DIEDNGPGIPPHLQDTLFY-- 302
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 18398532   712 eqadPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVV 746
Cdd:PRK11073  303 ----PMVSGREGGTGLGLSIARNLIDQHSGKIEFT 333
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
674-745 1.47e-04

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: 43.00  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  674 NHLQKSCKNANKMV----------LWFEVDDTGCGIDPSKWDSVFESFEQADPSttrtHGGTGLGLCIVRNLVNKMGGEI 743
Cdd:cd16954   44 NLLDNACKWCLEFVevtarqtdggLHLIVDDDGPGVPESQRSKIFQRGQRLDEQ----RPGQGLGLAIAKEIVEQYGGEL 119

                 ..
gi 18398532  744 KV 745
Cdd:cd16954  120 SL 121
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1044-1153 1.51e-04

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: 42.96  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKMG--ATVTAVWDGQQAVDSlnyksINAQAPteehksfeeetankvttretslrnsspy 1121
Cdd:COG2197    2 IRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALEL-----LEELRP---------------------------- 48
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18398532 1122 DLILMDCQMPKMDGYEATKAI--RR--------------AEIGTELHI 1153
Cdd:COG2197   49 DVVLLDIRMPGMDGLEALRRLltPRerevlrllaeglsnKEIAERLGI 96
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1044-1185 1.70e-04

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 44.42  E-value: 1.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1044 IRILLAEDTPVLQRVATIMLEKM-GATVTAVW-DGQQAVDSLnyksinaqaptEEHKsfeeetankvttretslrnsspY 1121
Cdd:COG3279    2 MKILIVDDEPLARERLERLLEKYpDLEVVGEAsNGEEALELL-----------EEHK----------------------P 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHamsSDEA-KCLEVGMDAYLTKPIDR 1185
Cdd:COG3279   49 DLVFLDIQMPGLDGFELARQLRELDP----PPPIIFTTAY---DEYAlEAFEVNAVDYLLKPIDE 106
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1044-1145 1.86e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 45.26  E-value: 1.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGAtVTAVW---DGQQAVDSlnyksINAQAPteehksfeeetankvttretslrnssp 1120
Cdd:PRK12555    1 MRIGIVNDSPLAVEALRRALARDPD-HEVVWvatDGAQAVER-----CAAQPP--------------------------- 47
                          90       100
                  ....*....|....*....|....*
gi 18398532  1121 yDLILMDCQMPKMDGYEATKAIRRA 1145
Cdd:PRK12555   48 -DVILMDLEMPRMDGVEATRRIMAE 71
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
612-750 2.77e-04

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: 41.68  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  612 DSARLVQIFANLISNSIKFTTTGHIIlrgwceninslhdemSVSVdrrkpwapmktkqvqhrnHLQKSCknankmvLWFE 691
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTV---------------SISI------------------YDEEEY-------LYFE 40
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532  692 VDDTGCGIDPSKWDSVFESFEQADpsTTRTHGG-TGLGLCIVRNLVNKMGGEIKV--VQKNG 750
Cdd:cd16975   41 IWDNGHGFSEQDLKKALELFYRDD--TSRRSGGhYGMGLYIAKNLVEKHGGSLIIenSQKGG 100
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1122-1182 3.69e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 43.25  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK10529   47 DLIILDLGLPDGDGIEFIRDLRQWS-----AIPVIVLSARSEESDKIAALDAGADDYLSKP 102
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
692-743 4.77e-04

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 44.24  E-value: 4.77e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18398532   692 VDDTGCGIDPSKWDSVFESFEQADpsTTRThgGTGLGLCIVRNLVNKMGGEI 743
Cdd:PRK10815  413 VEDDGPGIPESKRELIFDRGQRAD--TLRP--GQGLGLSVAREITEQYEGKI 460
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1046-1192 5.56e-04

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: 40.72  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQR--VATIMLEKMGATVTAVWDGQQAVDSLnyksinaqaptEEHKSfeeetankvttretslrnsspyDL 1123
Cdd:cd19930    1 VLIAEDQEMVRGalAALLELEDDLEVVAQASNGQEALRLV-----------LKHSP----------------------DV 47
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1124 ILMDCQMPKMDGYEATKAIRRAEIGTElhipIVALTAHAMSSDEAKCLEVGMDAYLTK--PIDRklMVSTI 1192
Cdd:cd19930   48 AILDIEMPGRTGLEVAAELREELPDTK----VLIVTTFGRPGYFRRALAAGVDGYVLKdrPIEE--LADAI 112
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
611-750 5.69e-04

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: 40.72  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  611 GDSARLVQIFANLISNSIKFTTTGhiilRGWCEninslhdemsVSVDRRKpwapmktKQVQHRNHLqkscknankMVLWF 690
Cdd:cd16932    2 GDQIRLQQVLADFLLNAVRFTPSP----GGWVE----------IKVSPTK-------KQIGDGVHV---------IHLEF 51
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  691 EVDDTGCGIDPSKWDSVFESfeqaDPSTTRthggTGLGLCIVRNLVNKMGGEIKVVQKNG 750
Cdd:cd16932   52 RITHPGQGLPEELVQEMFEE----NQWTTQ----EGLGLSISRKLVKLMNGDVRYLREAG 103
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1117-1192 6.93e-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: 40.60  E-value: 6.93e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1117 NSSPYDLILMDCQMPKMDGYEATKAIRRaeigtELHIP-IVALTAHamssDE--AKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17532   41 EELKPDVVFLDIQMPGLDGLELAKKLSK-----LAKPPlIVFVTAY----DEyaVEAFELNAVDYLLKPFSEERLAEAL 110
PRK10816 PRK10816
two-component system response regulator PhoP;
1044-1182 8.16e-04

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 42.42  E-value: 8.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1044 IRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAvdslnyksinaqapteehksfeeetankvttrETSLRNSSPyDL 1123
Cdd:PRK10816    1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEA--------------------------------DYYLNEHLP-DI 47
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  1124 ILMDCQMPKMDGyeaTKAIRRAEiGTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKP 1182
Cdd:PRK10816   48 AIVDLGLPDEDG---LSLIRRWR-SNDVSLPILVLTARESWQDKVEVLSAGADDYVTKP 102
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1121-1184 1.36e-03

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 42.71  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532  1121 YDLILMDCQMPKMDGYEATKAIRRAEIGtelhIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:PRK10365   50 FDLVLCDVRMAEMDGIATLKEIKALNPA----IPVLIMTAYSSVETAVEALKTGALDYLIKPLD 109
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1117-1184 1.50e-03

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: 39.56  E-value: 1.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1117 NSSPYDLILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPID 1184
Cdd:cd19919   41 ASSQPDVLISDIRMPGMDGLALLAQIKQRHP----DLPVIIMTAHSDLDSAVSAYQGGAFEYLPKPFD 104
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
691-759 1.56e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 42.51  E-value: 1.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532   691 EVDDTGCGIDPSKWDSVFEsfeQADPSTTRTHGGTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:PRK15053  472 EVADQGCGVPESLRDKIFE---QGVSTRADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFI 537
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
691-749 1.86e-03

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: 38.91  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532  691 EVDDTGCGIDPSKWDSVFESFEQADPSttRTHGGTGLGLCIVRNLVNKMGGEIKVVQKN 749
Cdd:cd16923   36 MFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSIAKAIIELHGGSASAEYDD 92
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
1040-1135 3.03e-03

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 41.81  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532  1040 SLEGIRILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVdslnyksinaqapteehksfeeetankvttreTSLRNSS 1119
Cdd:PRK11466  678 RLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQAL--------------------------------ETLQNSE 725
                          90
                  ....*....|....*.
gi 18398532  1120 PYDLILMDCQMPKMDG 1135
Cdd:PRK11466  726 PFAAALVDFDLPDYDG 741
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
692-759 3.92e-03

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: 38.29  E-value: 3.92e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532  692 VDDTGCGIDPSKWDSVFESFeqadpSTTRTHGgTGLGLCIVRNLVNKMGGEIKVVQKNGLGTLMRLYL 759
Cdd:cd16944   46 VCDNGKGFPREMRHRATEPY-----VTTRPKG-TGLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1124-1194 3.97e-03

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 38.34  E-value: 3.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18398532 1124 ILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHA---MSsdeAKCLEVGMDAYLTKPIDRKLMVSTILS 1194
Cdd:cd17537   48 LVLDVRMPGMSGLELQDELLARGS----NIPIIFITGHGdvpMA---VEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1114-1192 4.49e-03

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 38.18  E-value: 4.49e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18398532 1114 SLRNsspYDLILMDCQMPKMDGYEATKAIRRaeigTELHIPIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTI 1192
Cdd:cd17573   39 DIRN---YDLVLVSDKLPDGNGLSIVSRIKE----KHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1124-1192 6.36e-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: 39.31  E-value: 6.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18398532 1124 ILMDCQMPKMDGYEATKAIRRAEIgtelHIPIVALTAHAmssdeakclEVGM--DA-------YLTKPIDRKLMVSTI 1192
Cdd:COG4566   47 LLLDVRMPGMSGLELQEELAARGS----PLPVIFLTGHG---------DVPMavRAmkagavdFLEKPFDDQALLDAV 111
PRK10693 PRK10693
two-component system response regulator RssB;
1122-1183 6.70e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.97  E-value: 6.70e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532  1122 DLILMDCQMPKMDGYEATKAIRRAEIGTelhiPIVALTAHAMSSDEAKCLEVGMDAYLTKPI 1183
Cdd:PRK10693   19 DLIICDLAMPRMNGIEFVEHLRNRGDQT----PVLVISATENMADIAKALRLGVQDVLLKPV 76
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1046-1185 7.50e-03

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: 37.43  E-value: 7.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18398532 1046 ILLAEDTPVLQRVATIMLEKMGATVTAVWDGQQAVDSLNYKSInaqapteehksfeeetankvttretslrnsspyDLIL 1125
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRV---------------------------------DLVL 48
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18398532 1126 MDCQMPKMDGYEATKAIRRAEigtelHIPIVALTAHAM-SSDEAKCLEVGMDAYLTKPIDR 1185
Cdd:cd17594   49 LDLRLGQESGLDLLRTIRARS-----DVPIIIISGDRRdEIDRVVGLELGADDYLAKPFGL 104
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1122-1193 9.38e-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: 9.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18398532 1122 DLILMDCQMPKMDGYEATKAIRRAEIGTElhipIVALTAHAMSSDEAKCLEVGMDAYLTKPIDRKLMVSTIL 1193
Cdd:cd19931   46 DLILLDLNMKGMSGLDTLKALREEGVSAR----IVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
 
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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