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Conserved domains on  [gi|1934323370|ref|WP_195531129|]
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GAF domain-containing hybrid sensor histidine kinase/response regulator [Fusicatenibacter saccharivorans]

Protein Classification

GAF domain-containing hybrid sensor histidine kinase/response regulator( domain architecture ID 13662588)

GAF domain-containing hybrid sensor histidine kinase/response regulator, part of a two-component regulatory system, receives the signal from the sensor partner in a 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];
246-574 1.41e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 214.77  E-value: 1.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 246 RLPTAFAAQEEREKYREFLDFDTLTERLRNTNSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELM 325
Cdd:COG0642    14 LLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 326 YQKQLKEsmEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDvvKLRECRKKVLQSADYLQNLINNVLDIGK 405
Cdd:COG0642    94 LLLLALL--LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDE--EQREYLETILRSADRLLRLINDLLDLSR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 406 LESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVN 485
Cdd:COG0642   170 LEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP---TVRGDPDRLRQVLLNLLSNAIKYTPEGGTVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 486 VHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGS 565
Cdd:COG0642   247 VSVRREGDRVRISV-----EDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*....
gi 1934323370 566 TFTVTVPFE 574
Cdd:COG0642   320 TFTVTLPLA 328
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
593-723 1.18e-44

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: 156.16  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlERE 672
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIR--ALP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 673 DAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
GAF COG2203
GAF domain [Signal transduction mechanisms];
19-274 9.96e-12

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 68.30  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  19 TILHQISlmDQVENEQELSEIIHSLLQAIGNYTGADRVYVFDWETDQkdslsNTFEWCAdGVAPEIDNLQAIPVSSMPnW 98
Cdd:COG2203   193 ALLNEIS--QALRSALDLEELLQRILELAGELLGADRGAILLVDEDG-----GELELVA-APGLPEEELGRLPLGEGL-A 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  99 VKRFENKEVIVIHDLEATKNSEPEEYELLKTQEICSLIAVPIYANHQMNGFIGVDNPDLRQ-NEISITLLSDVGGHLGCV 177
Cdd:COG2203   264 GRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAfTEEDLELLEALADQAAIA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 178 RENLKSTVLLKKALDEATKRSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEER 257
Cdd:COG2203   344 IERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLL 423
                         250
                  ....*....|....*..
gi 1934323370 258 EKYREFLDFDTLTERLR 274
Cdd:COG2203   424 LDLLLLLLLLRRILLLR 440
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
246-574 1.41e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 214.77  E-value: 1.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 246 RLPTAFAAQEEREKYREFLDFDTLTERLRNTNSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELM 325
Cdd:COG0642    14 LLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 326 YQKQLKEsmEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDvvKLRECRKKVLQSADYLQNLINNVLDIGK 405
Cdd:COG0642    94 LLLLALL--LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDE--EQREYLETILRSADRLLRLINDLLDLSR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 406 LESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVN 485
Cdd:COG0642   170 LEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP---TVRGDPDRLRQVLLNLLSNAIKYTPEGGTVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 486 VHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGS 565
Cdd:COG0642   247 VSVRREGDRVRISV-----EDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*....
gi 1934323370 566 TFTVTVPFE 574
Cdd:COG0642   320 TFTVTLPLA 328
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
337-720 4.27e-59

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: 215.80  E-value: 4.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 337 AHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKynndvVKLRECRKKVLQ----SADYLQNLINNVLDIGKLESGSLV 412
Cdd:TIGR02956 457 AEEANRAKSAFLATMSHEIRTPLNGILGTLELLGD-----TGLTSQQQQYLQvinrSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 413 LEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTirHRYLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNVHCeELS 492
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQL--PNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRV-SLN 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 493 DDGNIAvfqFVCSDTGLGMSEEFQKHAFDAFAQ-EGKQSTttfSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTV 571
Cdd:TIGR02956 608 DDSSLL---FEVEDTGCGIAEEEQATLFDAFTQaDGRRRS---GGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL 681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 572 PfeidyLAENNDSQKDSYSQDMDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMD 651
Cdd:TIGR02956 682 P-----LTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA---FDLALLD 753
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934323370 652 VMMPVMDGLEATKAIRMLEREDaKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:TIGR02956 754 INLPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
337-718 5.72e-53

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 197.38  E-value: 5.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 337 AHRANLSKTAFLRRMSHDIRTPLNGIVGmihiaekYNNDVVK--LRECRKKVLQ----SADYLQNLINNVLDIGKLESGS 410
Cdd:PRK11107  286 AQEAARIKSEFLANMSHELRTPLNGVIG-------FTRQTLKtpLTPTQRDYLQtierSANNLLAIINDILDFSKLEAGK 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 411 LVLEHKSFDLAELLRNNLTVVAMSAYENGVrfeggvEAS-TIRHR---YLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNV 486
Cdd:PRK11107  359 LVLENIPFSLRETLDEVVTLLAHSAHEKGL------ELTlNIDPDvpdNVIGDPLRLQQIITNLVGNAIKFTE-SGNIDI 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 487 HCEELSDDGNIAVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGST 566
Cdd:PRK11107  432 LVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGST 511
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 567 FTVTVPFEI-----------DYLA-------ENN-----------------------DSQKDSYSQDMDLSGK------- 598
Cdd:PRK11107  512 FWFHLPLDLnpnpiidglptDCLAgkrllyvEPNsaaaqatldilsetplevtysptLSQLPEAHYDILLLGLpvtfrep 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 -----------------------------------------------------------------------------RVL 601
Cdd:PRK11107  592 ltmlherlakaksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVM 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 602 LVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRMLEREdaKKIPIIA 681
Cdd:PRK11107  672 AVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRP---FDLILMDIQMPGMDGIRACELIRQLPHN--QNTPIIA 746
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1934323370 682 MTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITK 718
Cdd:PRK11107  747 VTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLR 783
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
593-723 1.18e-44

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: 156.16  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlERE 672
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIR--ALP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 673 DAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
600-716 3.09e-44

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: 154.55  E-value: 3.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRMLEReDAKKIPI 679
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE---EPFDLVLMDLQMPVMDGLEATRRIRELEG-GGRRTPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:cd17546    77 IALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
466-573 2.97e-33

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 123.37  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 466 VLMNLSSNAIKYNHfHGTVNVHCEELSDDGNIAVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVK 545
Cdd:cd16922     4 ILLNLLGNAIKFTE-EGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 1934323370 546 DIVERMGGTIELESEENVGSTFTVTVPF 573
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
600-716 1.06e-29

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: 113.40  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlerEDAKKIPI 679
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---PDLILLDINMPGMDGLELLKRIR----RRDPTTPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
458-574 3.03e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.97  E-value: 3.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQeGKQSTTTFSGS 537
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITV-----EDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1934323370  538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
458-575 1.14e-26

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: 104.76  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVhceELSDDGNIavfQFVCSDTGLGMSEEFQKHAFDAFAQegkQSTTTFSGS 537
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITV---TLSEGGEL---TLTVEDNGIGIPPEDLPRIFEPFST---ADKRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1934323370 538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFEI 575
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
599-720 9.12e-14

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 74.11  E-value: 9.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLV--EDNVINMeiAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLERedakK 676
Cdd:PRK11361    6 RILIVddEDNVRRM--LSTAFALQGFETHCANNGRTALHLFADIHPD---VVLMDIRMPEMDGIKALKEMRSHET----R 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK11361   77 TPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
598-655 2.14e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.20  E-value: 2.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1934323370  598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMP 655
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE---EKPDLILLDIMMP 55
GAF COG2203
GAF domain [Signal transduction mechanisms];
19-274 9.96e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 68.30  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  19 TILHQISlmDQVENEQELSEIIHSLLQAIGNYTGADRVYVFDWETDQkdslsNTFEWCAdGVAPEIDNLQAIPVSSMPnW 98
Cdd:COG2203   193 ALLNEIS--QALRSALDLEELLQRILELAGELLGADRGAILLVDEDG-----GELELVA-APGLPEEELGRLPLGEGL-A 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  99 VKRFENKEVIVIHDLEATKNSEPEEYELLKTQEICSLIAVPIYANHQMNGFIGVDNPDLRQ-NEISITLLSDVGGHLGCV 177
Cdd:COG2203   264 GRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAfTEEDLELLEALADQAAIA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 178 RENLKSTVLLKKALDEATKRSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEER 257
Cdd:COG2203   344 IERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLL 423
                         250
                  ....*....|....*..
gi 1934323370 258 EKYREFLDFDTLTERLR 274
Cdd:COG2203   424 LDLLLLLLLLRRILLLR 440
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
35-175 7.43e-08

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 51.71  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  35 ELSEIIHSLLQAIGNYTGADRVYVFDWETDQKDSLSNTFEW--CADGVAPEIDNLQAipvssmpnwvkrFENKEVIVIHD 112
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWlkAAGLEIPPGTGVTV------------LRTGRPLVVPD 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 113 LEATkNSEPEEYELLKTQEICSLIAVPIYANHQMNGFIGVDNPDLRQNEISITLLSDVGGHLG 175
Cdd:pfam01590  69 AAGD-PRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPFTEEELELLEVLADQVA 130
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
36-175 5.22e-06

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.99  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370   36 LSEIIHSLLQAIGNYTGADRVYVFDWETDQKDSLSnTFEWCADGVAPEIdnlQAIPVSSMP-NWVkrFENKEVIVIHDLE 114
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELV-LVAADGLTLPTLG---IRFPLDEGLaGRV--AETGRPLNIPDVE 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934323370  115 AtknsEPEEYELLKTQEIC--SLIAVPIYANHQMNGFIGVDNPDLRQ--NEISITLLSDVGGHLG 175
Cdd:smart00065  76 A----DPLFAEDLLGRYQGvrSFLAVPLVADGELVGVLALHNKKSPRpfTEEDEELLQALANQLA 136
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
246-574 1.41e-63

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 214.77  E-value: 1.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 246 RLPTAFAAQEEREKYREFLDFDTLTERLRNTNSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELM 325
Cdd:COG0642    14 LLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 326 YQKQLKEsmEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDvvKLRECRKKVLQSADYLQNLINNVLDIGK 405
Cdd:COG0642    94 LLLLALL--LLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDE--EQREYLETILRSADRLLRLINDLLDLSR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 406 LESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVN 485
Cdd:COG0642   170 LEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP---TVRGDPDRLRQVLLNLLSNAIKYTPEGGTVT 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 486 VHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGS 565
Cdd:COG0642   247 VSVRREGDRVRISV-----EDTGPGIPPEDLERIFEPFFRTD--PSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGT 319

                  ....*....
gi 1934323370 566 TFTVTVPFE 574
Cdd:COG0642   320 TFTVTLPLA 328
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
329-572 1.33e-59

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 200.90  E-value: 1.33e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 329 QLKESMEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVV-KLRECRKKVLQSADYLQNLINNVLDIGKLE 407
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPeERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 408 SGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVH 487
Cdd:COG2205    81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP---LVYADPELLEQVLANLLDNAIKYSPPGGTITIS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 488 CEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTF 567
Cdd:COG2205   158 ARREGDGVRISV-----SDNGPGIPEEELERIFERFYRGD--NSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTF 230

                  ....*
gi 1934323370 568 TVTVP 572
Cdd:COG2205   231 TVTLP 235
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
337-720 4.27e-59

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: 215.80  E-value: 4.27e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 337 AHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKynndvVKLRECRKKVLQ----SADYLQNLINNVLDIGKLESGSLV 412
Cdd:TIGR02956 457 AEEANRAKSAFLATMSHEIRTPLNGILGTLELLGD-----TGLTSQQQQYLQvinrSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 413 LEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTirHRYLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNVHCeELS 492
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQL--PNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRV-SLN 607
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 493 DDGNIAvfqFVCSDTGLGMSEEFQKHAFDAFAQ-EGKQSTttfSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTV 571
Cdd:TIGR02956 608 DDSSLL---FEVEDTGCGIAEEEQATLFDAFTQaDGRRRS---GGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTL 681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 572 PfeidyLAENNDSQKDSYSQDMDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMD 651
Cdd:TIGR02956 682 P-----LTRGKPAEDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHA---FDLALLD 753
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934323370 652 VMMPVMDGLEATKAIRMLEREDaKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:TIGR02956 754 INLPDGDGVTLLQQLRAIYGAK-NEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
200-572 1.72e-53

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 189.38  E-value: 1.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 200 IIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEEREKYREFLDFDTLTERLRNTNSV 279
Cdd:COG5002    21 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 280 SIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELMYQKQLKESMEDAHRANLSKTAFLRRMSHDIRTPL 359
Cdd:COG5002   101 LLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 360 NGIVGMIH-IAEKYNNDVVKLRECRKKVLQSADYLQNLINNVLDIGKLESGSLVLEHKSFDLAELLRNNLTVVAMSAYEN 438
Cdd:COG5002   181 TSIRGYLElLLDGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEK 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 439 GVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKH 518
Cdd:COG5002   261 GIELELDLPEDPL---LVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDDQVRISV-----RDTGIGIPEEDLPR 332
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 519 AFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG5002   333 IFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLP 386
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
337-718 5.72e-53

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 197.38  E-value: 5.72e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 337 AHRANLSKTAFLRRMSHDIRTPLNGIVGmihiaekYNNDVVK--LRECRKKVLQ----SADYLQNLINNVLDIGKLESGS 410
Cdd:PRK11107  286 AQEAARIKSEFLANMSHELRTPLNGVIG-------FTRQTLKtpLTPTQRDYLQtierSANNLLAIINDILDFSKLEAGK 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 411 LVLEHKSFDLAELLRNNLTVVAMSAYENGVrfeggvEAS-TIRHR---YLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNV 486
Cdd:PRK11107  359 LVLENIPFSLRETLDEVVTLLAHSAHEKGL------ELTlNIDPDvpdNVIGDPLRLQQIITNLVGNAIKFTE-SGNIDI 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 487 HCEELSDDGNIAVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGST 566
Cdd:PRK11107  432 LVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGST 511
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 567 FTVTVPFEI-----------DYLA-------ENN-----------------------DSQKDSYSQDMDLSGK------- 598
Cdd:PRK11107  512 FWFHLPLDLnpnpiidglptDCLAgkrllyvEPNsaaaqatldilsetplevtysptLSQLPEAHYDILLLGLpvtfrep 591
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 -----------------------------------------------------------------------------RVL 601
Cdd:PRK11107  592 ltmlherlakaksmtdflilalpcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdesrlplTVM 671
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 602 LVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRMLEREdaKKIPIIA 681
Cdd:PRK11107  672 AVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRP---FDLILMDIQMPGMDGIRACELIRQLPHN--QNTPIIA 746
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1934323370 682 MTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITK 718
Cdd:PRK11107  747 VTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLR 783
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
314-719 5.88e-52

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 193.23  E-value: 5.88e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 314 RDITEEKSrelmYQkqlkESMEDAHRanlSKTAFLRRMSHDIRTPLNGIVGMIHI---------AEKYnndvvklrecRK 384
Cdd:PRK11091  264 RDITERKR----YQ----DALEKASR---DKTTFISTISHELRTPLNGIVGLSRIlldteltaeQRKY----------LK 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 385 KVLQSADYLQNLINNVLDIGKLESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEggVEASTIRHRYLIGSPVHLS 464
Cdd:PRK11091  323 TIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFD--LEPLLPLPHKVITDGTRLR 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 465 RVLMNLSSNAIKYNHfHGTVNVHCEELSDDgniaVFQFVCSDTGLGMSEEFQKHAFDAFAQ----EGKQSTTtfsGSGLG 540
Cdd:PRK11091  401 QILWNLISNAVKFTQ-QGGVTVRVRYEEGD----MLTFEVEDSGIGIPEDELDKIFAMYYQvkdsHGGKPAT---GTGIG 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 541 LSIVKDIVERMGGTIELESEENVGSTFTVTVPFEIdyLAENNDSQKDsySQDMDLSGKRVLLVEDNVINMEIAHAILEEE 620
Cdd:PRK11091  473 LAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPA--VAEEVEDAFD--EDDMPLPALNILLVEDIELNVIVARSVLEKL 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 621 HLNITEAKNGKEAFEIFqnsRLDEYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKI-PIIAMTANAFeEDRKACLEAGM 699
Cdd:PRK11091  549 GNSVDVAMTGKEALEMF---DPDEYDLVLLDIQLPDMTGLDIARELR--ERYPREDLpPLVALTANVL-KDKKEYLDAGM 622
                         410       420
                  ....*....|....*....|
gi 1934323370 700 NEHIGKPIDIPRLKRAITKL 719
Cdd:PRK11091  623 DDVLSKPLSVPALTAMIKKF 642
PRK15347 PRK15347
two component system sensor kinase;
329-716 1.06e-50

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 190.62  E-value: 1.06e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 329 QLKESMEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVvKLRECRKKVLQSADYLQNLINNVLDIGKLES 408
Cdd:PRK15347  383 ALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTA-EQMDLADTARQCTLSLLAIINNLLDFSRIES 461
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 409 GSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTirHRYLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNVHC 488
Cdd:PRK15347  462 GQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHV--PLYLHLDSLRLRQILVNLLGNAVKFTE-TGGIRLRV 538
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 489 EELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQegkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFT 568
Cdd:PRK15347  539 KRHEQQLCFTV-----EDTGCGIDIQQQQQIFTPFYQ----ADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFS 609
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 569 VTVPFEiDYLA--------------------------ENNDSQKDSYSQDMDLSGK------------------------ 598
Cdd:PRK15347  610 LVLPLN-EYAPpeplkgelsaplalhrqlsawgitcqPGHQNPALLDPELAYLPGRlydllqqiiqgapnepvinlplqp 688
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 ---RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKairmLEREDAK 675
Cdd:PRK15347  689 wqlQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHR---FDLVLMDIRMPGLDGLETTQ----LWRDDPN 761
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1934323370 676 KI----PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:PRK15347  762 NLdpdcMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL 806
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
593-723 1.18e-44

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: 156.16  E-value: 1.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlERE 672
Cdd:COG0784     1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGP---PDLILLDINMPGMDGLELLRRIR--ALP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 673 DAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG0784    76 RLPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARA 126
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
600-716 3.09e-44

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: 154.55  E-value: 3.09e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRMLEReDAKKIPI 679
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE---EPFDLVLMDLQMPVMDGLEATRRIRELEG-GGRRTPI 76
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:cd17546    77 IALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
314-719 4.42e-44

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 171.46  E-value: 4.42e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  314 RDITEekSRELMYQKQLKESmeDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKKVLQSADYL 393
Cdd:PRK09959   686 QDITE--TRDLIHALEVERN--KAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAISLAYATGQSL 761
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  394 QNLINNVLDIGKLESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGgveASTIRHRYLIG-SPVHLSRVLMNLSS 472
Cdd:PRK09959   762 LGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC---SSTFPDHYLVKiDPQAFKQVLSNLLS 838
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  473 NAIKYNHfHGTVNVHCEELSDDGNIAVFQFVCSDTGLGMSEEFQKHAFDAFAQE--GKQSTttfsGSGLGLSIVKDIVER 550
Cdd:PRK09959   839 NALKFTT-EGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTsaGRQQT----GSGLGLMICKELIKN 913
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  551 MGGTIELESEENVGSTFTVTVPFEIDYLAENNDSQKDsysQDMDLSGK-RVLLVEDNVINMEIAHAILEEEHLNITEAKN 629
Cdd:PRK09959   914 MQGDLSLESHPGIGTTFTITIPVEISQQVATVEAKAE---QPITLPEKlSILIADDHPTNRLLLKRQLNLLGYDVDEATD 990
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  630 GKEAfeiFQNSRLDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDI 709
Cdd:PRK09959   991 GVQA---LHKVSMQHYDLLITDVNMPNMDGFELTRKL----REQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTL 1063
                          410
                   ....*....|
gi 1934323370  710 PRLKRAITKL 719
Cdd:PRK09959  1064 DVLKTHLSQL 1073
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
186-572 1.83e-38

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 149.94  E-value: 1.83e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 186 LLKKALDEATKRSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEEREKYREFLD 265
Cdd:COG4251   121 LLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLL 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 266 FDTLTERLRNTNSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELM---YQKQLKESMEDAHRANL 342
Cdd:COG4251   201 LLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLEleeLEEELEERTAELERSNE 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 343 SKTAFLRRMSHDIRTPLNGIVGMIH-IAEKYNNDVV-KLRECRKKVLQSADYLQNLINNVLDIGKLESGSLVLEHksFDL 420
Cdd:COG4251   281 ELEQFAYVASHDLREPLRKISGFSQlLEEDYGDKLDeEGREYLERIRDAAERMQALIDDLLAYSRVGRQELEFEP--VDL 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 421 AELLRNNLTVVAMSAYENGVRFEGGvEASTIRhryliGSPVHLSRVLMNLSSNAIKYNH--FHGTVNVHCEELSDDgnia 498
Cdd:COG4251   359 NELLEEVLEDLEPRIEERGAEIEVG-PLPTVR-----GDPTLLRQVFQNLISNAIKYSRpgEPPRIEIGAEREGGE---- 428
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 499 vFQFVCSDTGLGMSEEFQKHAFDAFAQegKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG4251   429 -WVFSVRDNGIGIDPEYAEKIFEIFQR--LHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLP 499
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
599-716 2.06e-35

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: 131.95  E-value: 2.06e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHR---PDLILLDLEMPDMDGLELCRRLR--ADPRTADIP 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:COG3706    78 IIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
197-572 2.64e-34

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 134.54  E-value: 2.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 197 RSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEEREKYREFLDFDTLTERLRNT 276
Cdd:COG4191     2 LRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 277 NSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELmyQKQLKESmedahranlSKTAFLRRMS---- 352
Cdd:COG4191    82 LGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELREL--QEQLVQS---------EKLAALGELAagia 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 353 HDIRTPLNGIVGMIHIAEKY---NNDVVKLRECRKKVLQSADYLQNLINNVLDIGKLESgslvLEHKSFDLAELLRNNLT 429
Cdd:COG4191   151 HEINNPLAAILGNAELLRRRledEPDPEELREALERILEGAERAAEIVRSLRAFSRRDE----EEREPVDLNELIDEALE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 430 VVAMSAYENGVRFEGGVEASTIRhryLIGSPVHLSRVLMNLSSNAIK--YNHFHGTVNVHCEELSDDGNIAVfqfvcSDT 507
Cdd:COG4191   227 LLRPRLKARGIEVELDLPPDLPP---VLGDPGQLEQVLLNLLINAIDamEEGEGGRITISTRREGDYVVISV-----RDN 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934323370 508 GLGMSEEFQKHAFDAFAqegkqsTT--TFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG4191   299 GPGIPPEVLERIFEPFF------TTkpVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
466-573 2.97e-33

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 123.37  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 466 VLMNLSSNAIKYNHfHGTVNVHCEELSDDGNIAVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVK 545
Cdd:cd16922     4 ILLNLLGNAIKFTE-EGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISK 82
                          90       100
                  ....*....|....*....|....*...
gi 1934323370 546 DIVERMGGTIELESEENVGSTFTVTVPF 573
Cdd:cd16922    83 KLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
331-720 9.71e-33

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 135.80  E-value: 9.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 331 KESMEDAHRANLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKyNNDVVKLRECRKKVLQSADYLQNLINNVLDIGKLESG- 409
Cdd:PRK11466  431 RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLAD-NPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGg 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 410 -SLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEggVEASTIRHRYLIGSPVHLSRVLMNLSSNAIKYNHfHGTVNVHC 488
Cdd:PRK11466  510 kNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLA--TDIADDLPTALMGDPRRIRQVITNLLSNALRFTD-EGSIVLRS 586
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 489 EELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAqegkQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFT 568
Cdd:PRK11466  587 RTDGEQWLVEV-----EDSGCGIDPAKLAEIFQPFV----QVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFC 657
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 569 VTVPFEIDYLAEnndsqKDSYSQDMDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrlDEYDVI 648
Cdd:PRK11466  658 LRLPLRVATAPV-----PKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQNS--EPFAAA 730
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934323370 649 IMDVMMPVMDGLeaTKAIRMLEREDAKKipIIAMTANAFEED---RKACLEAGMnehIGKPIDIPRLKRAITKLL 720
Cdd:PRK11466  731 LVDFDLPDYDGI--TLARQLAQQYPSLV--LIGFSAHVIDETlrqRTSSLFRGI---IPKPVPREVLGQLLAHYL 798
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
327-717 2.43e-31

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 131.25  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 327 QKQLKESMEDAHRANLSKTAFLRRMSHDIRTPLNGIVGmihiaekyNNDVVKLRECRKKVLQ-------SADYLQNLINN 399
Cdd:PRK10841  430 EESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIG--------NLDLLQTKELPKGVDRlvtamnnSSSLLLKIISD 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 400 VLDIGKLESGSLVLEHKSFDLAELLR----NNLTVVAMSAYENGVRFEGGVEastirhRYLIGSPVHLSRVLMNLSSNAI 475
Cdd:PRK10841  502 ILDFSKIESEQLKIEPREFSPREVINhitaNYLPLVVKKRLGLYCFIEPDVP------VALNGDPMRLQQVISNLLSNAI 575
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 476 KYNHFHGTV-NVHCeelsDDGNIAvfqFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGT 554
Cdd:PRK10841  576 KFTDTGCIVlHVRV----DGDYLS---FRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGD 648
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 555 IELESEENVGSTFTVTVP-------------------------------FEIDYLAENN--------------------- 582
Cdd:PRK10841  649 ISVDSEPGMGSQFTIRIPlygaqypqkkgveglqgkrcwlavrnasleqFLETLLQRSGiqvqryegqeptpedvlitdd 728
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 583 DSQKDS-----------------------------------------YSQDMDLSGK-----------------RVLLVE 604
Cdd:PRK10841  729 PVQKKWqgravitfcrrhigipleiapgewvhstatphelpallariYRIELESDDSanalpstdkavsdnddmMILVVD 808
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 605 DNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPIIAMTA 684
Cdd:PRK10841  809 DHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK---NHIDIVLTDVNMPNMDGYRLTQRL----RQLGLTLPVIGVTA 881
                         490       500       510
                  ....*....|....*....|....*....|...
gi 1934323370 685 NAFEEDRKACLEAGMNEHIGKPIDIPRLKRAIT 717
Cdd:PRK10841  882 NALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLT 914
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
598-720 8.99e-31

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: 119.68  E-value: 8.99e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlerEDAKKI 677
Cdd:COG0745     2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEER---PDLILLDLMLPGMDGLEVCRRLR----ARPSDI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:COG0745    75 PIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
281-574 1.65e-30

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 123.42  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 281 IEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEeksrelmyQKQLKESMEDAHRANLSKTaFLRRMSHDIRTPLN 360
Cdd:COG3852    81 VTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITE--------RKRLERELRRAEKLAAVGE-LAAGLAHEIRNPLT 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 361 GIVGMI-HIAEKYNNDvvKLRECRKKVLQSADYLQNLINNVLDIGKLESgslvLEHKSFDLAELLRNNLTVVAmSAYENG 439
Cdd:COG3852   152 GIRGAAqLLERELPDD--ELREYTQLIIEEADRLNNLVDRLLSFSRPRP----PEREPVNLHEVLERVLELLR-AEAPKN 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 440 VRfeggveastIRHRY------LIGSPVHLSRVLMNLSSNAIKYNHFHGTV-----NVHCEELSDDGNIAVFQFVCSDTG 508
Cdd:COG3852   225 IR---------IVRDYdpslpeVLGDPDQLIQVLLNLVRNAAEAMPEGGTItirtrVERQVTLGGLRPRLYVRIEVIDNG 295
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1934323370 509 LGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:COG3852   296 PGIPEEILDRIFEPFF------TTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLE 355
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
599-718 3.63e-30

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: 114.94  E-value: 3.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPD---LILMDIQLPGMDGLEATRLLK--EDPATRDIP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITK 718
Cdd:cd17548    76 VIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
310-572 6.53e-30

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: 123.15  E-value: 6.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 310 LYVVRDITEEKSRELMyqkqlkESMEDahranlsktaFLRRMSHDIRTPLNGIVGMI-HIAEKYNNDVV----KLRECRK 384
Cdd:COG5000   183 VIVFDDITELLRAERL------AAWGE----------LARRIAHEIKNPLTPIQLSAeRLRRKLADKLEedreDLERALD 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 385 KVLQSADYLQNLINNVLDIGKLESgslvLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIRhryLIGSPVHLS 464
Cdd:COG5000   247 TIIRQVDRLKRIVDEFLDFARLPE----PQLEPVDLNELLREVLALYEPALKEKDIRLELDLDPDLPE---VLADRDQLE 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 465 RVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIV 544
Cdd:COG5000   320 QVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEV-----SDNGPGIPEEVLERIFEPFF------TTKPKGTGLGLAIV 388
                         250       260
                  ....*....|....*....|....*...
gi 1934323370 545 KDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG5000   389 KKIVEEHGGTIELESRPGGGTTFTIRLP 416
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
600-716 1.06e-29

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: 113.40  E-value: 1.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlerEDAKKIPI 679
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEER---PDLILLDINMPGMDGLELLKRIR----RRDPTTPV 73
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:pfam00072  74 IILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
458-574 3.03e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 111.97  E-value: 3.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQeGKQSTTTFSGS 537
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITV-----EDNGPGIPPEDLEKIFEPFFR-TDKRSRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1934323370  538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
596-723 7.80e-29

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: 114.88  E-value: 7.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 596 SGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlEREDAK 675
Cdd:COG3437     5 QAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAP---PDLILLDVRMPGMDGFELLRLLR--ADPSTR 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG3437    80 DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELR 127
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
458-575 1.14e-26

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: 104.76  E-value: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVhceELSDDGNIavfQFVCSDTGLGMSEEFQKHAFDAFAQegkQSTTTFSGS 537
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAKAGEITV---TLSEGGEL---TLTVEDNGIGIPPEDLPRIFEPFST---ADKRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1934323370 538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFEI 575
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
600-716 2.14e-26

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: 104.08  E-value: 2.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIPI 679
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFR---PDVILSDIGMPGMDGYELARRLR--ELPWLANTPA 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:cd17580    76 IALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
187-572 1.04e-25

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: 111.60  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 187 LKKALDEATKRSEIIAAIATLYVTIVqanvkERTYELLKGHDLVQKILGQKgkIDDVMERLPTAFAAQEEREKYREFLDf 266
Cdd:COG5809   132 MEEALRESEEKFRLIFNHSPDGIIVT-----DLDGRIIYANPAACKLLGIS--IEELIGKSILELIHSDDQENVAAFIS- 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 267 dtltERLRNTNSVSIE--FMGVNGEWRLARF----IVKSRDAHGNAVdvlyVVRDITEeksrelmyQKQLKESMEDAHRa 340
Cdd:COG5809   204 ----QLLKDGGIAQGEvrFWTKDGRWRLLEAsgapIKKNGEVDGIVI----IFRDITE--------RKKLEELLRKSEK- 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 341 nLSKTA-FLRRMSHDIRTPLNGIVGMIHIAEKYNNDvvklrecrkkvlQSADYLQ----------NLINNVLDIGKLESG 409
Cdd:COG5809   267 -LSVVGeLAAGIAHEIRNPLTSLKGFIQLLKDTIDE------------EQKTYLDimlseldrieSIISEFLVLAKPQAI 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 410 SLvlehKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCE 489
Cdd:COG5809   334 KY----EPKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIP---DILGDENQLKQVFINLLKNAIEAMPEGGNITIETK 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 490 ELSDDGNIAVFQfvcsDTGLGMSEEFQKHAFDAFaqegkqSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTV 569
Cdd:COG5809   407 AEDDDKVVISVT----DEGCGIPEERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSI 476

                  ...
gi 1934323370 570 TVP 572
Cdd:COG5809   477 TLP 479
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
601-706 2.12e-25

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 100.76  E-value: 2.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 601 LLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPII 680
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREER---PDLVLLDLMMPGMDGLELLRKL----RELPPDIPVI 73
                          90       100
                  ....*....|....*....|....*.
gi 1934323370 681 AMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd00156    74 VLTAKADEEDAVRALELGADDYLVKP 99
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
300-572 2.52e-25

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 111.21  E-value: 2.52e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 300 RDAHGNAVDVLYVVRDITEeksrelmyQKQLKESMEDAHR-ANLSKtaFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVVK 378
Cdd:PRK11360  355 HNTHGEMIGALVIFSDLTE--------RKRLQRRVARQERlAALGE--LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPS 424
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 379 lRECRKKVLQSADYLQNLINNVLDIGKLESGSLVlehkSFDLAELLRNNLTVVAMSAYENGVRFEGGVEAS--TIrhryl 456
Cdd:PRK11360  425 -QEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVEEVLQLFQTAGVQARVDFETELDNElpPI----- 494
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 457 IGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDgNIAVfqfVCSDTGLGMSEEFQKHAFDAFAqegkqsTTTFSG 536
Cdd:PRK11360  495 WADPELLKQVLLNILINAVQAISARGKIRIRTWQYSDG-QVAV---SIEDNGCGIDPELLKKIFDPFF------TTKAKG 564
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1934323370 537 SGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:PRK11360  565 TGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
601-706 7.61e-24

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: 96.32  E-value: 7.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 601 LLVEDNVinmEIAHAI---LEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd17574     1 LVVEDDE---EIAELLsdyLEKEGYEVDTAADGEEALELARE---EQPDLIILDVMLPGMDGFEVCRRL----REKGSDI 70
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17574    71 PIIMLTAKDEEEDKVLGLELGADDYITKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
596-723 2.50e-22

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: 100.04  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 596 SGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRmlerEDAK 675
Cdd:COG2204     1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE---EPPDLVLLDLRMPGMDGLELLRELR----ALDP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG2204    74 DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERR 121
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
599-707 7.02e-22

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: 91.02  E-value: 7.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPD---LILLDVMMPGMDGFEVCRRLK--EDPETRHIP 75
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPI 707
Cdd:cd17538    76 VIMITALDDREDRIRGLEAGADDFLSKPI 104
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
599-706 8.55e-22

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: 90.60  E-value: 8.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEE--HLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEagFEVVGEAENGEEALELLEEHK---PDLVITDINMPGMDGLELLEAI----RELDPD 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:COG4753    74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
303-574 9.78e-22

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 98.00  E-value: 9.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 303 HGNAVDVLYVVRDITEEKSRElMYQKQLKESMEDahranlsktafLRRMSHDIRTPLNGIVGMIHIaekynndvvklrec 382
Cdd:COG3290   160 DGRVVGAVATFRDRTELERLE-EELEGVKELAEA-----------LRAQRHDFRNHLHTISGLLQL-------------- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 383 rKKVLQSADYLQNLINNVLDIgkleSGSLVLEHKSFDLAELLRNNLTVvamsAYENGVRFEggVEASTIRHRYLIgSPVH 462
Cdd:COG3290   214 -GEYDEALEYIDEISEELQEL----IDSLLSRIGNPVLAALLLGKAAR----ARERGIDLT--IDIDSDLPDLPL-SDTD 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAI----KYNHFHGTVNVhceELSDDGNIAVFqfVCSDTGLGMSEEFQKHAFdafaqEGKQSTTTFSGSG 538
Cdd:COG3290   282 LVTILGNLLDNAIeaveKLPEEERRVEL---SIRDDGDELVI--EVEDSGPGIPEELLEKIF-----ERGFSTKLGEGRG 351
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1934323370 539 LGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:COG3290   352 LGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKE 387
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
598-721 7.07e-21

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: 88.70  E-value: 7.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNV-INMEIaHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:COG5803     3 KKILIVDDQAgIRMLL-KEVLKKEGYEVFQAANGKEALEKVKELK---PDLVLLDMKMPGMDGIEILKEI----KEIDPD 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLT 721
Cdd:COG5803    75 IPVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLLK 119
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
595-723 1.01e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 88.87  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 595 LSGKRVLLVEDNVINMEIAHAILE--EEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRmlerE 672
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLErlPGFEVVGVASSGEEALALLAE---HRPDLILLDIYLPDGDGLELLRELR----A 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 673 DAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG4565    74 RGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYR 124
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 2.41e-19

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 83.53  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNH--FHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGKQSTttFSGSGLG 540
Cdd:cd16921     1 LGQVLTNLLGNAIKFRRprRPPRIEVGAEDVGEEWTFYV-----RDNGIGIDPEYAEKVFGIFQRLHSREE--YEGTGVG 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934323370 541 LSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16921    74 LAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
PRK10490 PRK10490
sensor protein KdpD; Provisional
329-574 8.70e-19

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 91.25  E-value: 8.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 329 QLKESME----DAHRANLsKTAFLRRMSHDIRTPLNGIVG-----MIHIAEKYNNDVVKLRECRKKVLQSAdylqNLINN 399
Cdd:PRK10490  646 TLTASEEqarlASEREQL-RNALLAALSHDLRTPLTVLFGqaeilTLDLASEGSPHARQASEIRQQVLNTT----RLVNN 720
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 400 VLDIGKLESGSLVLEHKSFDLAELLRNnltvvAMSAYENGvrfeggveastirhryLIGSPVHLS--------------- 464
Cdd:PRK10490  721 LLDMARIQSGGFNLRKEWLTLEEVVGS-----ALQMLEPG----------------LSGHPINLSlpepltlihvdgplf 779
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 465 -RVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVFqfvcsDTGLGMSEEFQKHAFDAFAQEGKQSTttFSGSGLGLSI 543
Cdd:PRK10490  780 eRVLINLLENAVKYAGAQAEIGIDAHVEGERLQLDVW-----DNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAI 852
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1934323370 544 VKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:PRK10490  853 CRAIVEVHGGTIWAENRPEGGACFRVTLPLE 883
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
599-708 2.47e-18

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: 81.33  E-value: 2.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEE-EHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRMLEREDAkkI 677
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSaGYLEVVSFTDPREALAWCRE---NPPDLILLDYMMPGMDGLEFIRRLRALPGLED--V 76
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPID 708
Cdd:cd17551    77 PIVMITADTDREVRLRALEAGATDFLTKPFD 107
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
599-719 2.81e-18

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: 81.31  E-value: 2.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHL--NITEAKNGKEAFEIFQnsRLDEY------DVIIMDVMMPVMDGLEATKAIRmlE 670
Cdd:cd17557     1 TILLVEDNPGDAELIQEAFKEAGVpnELHVVRDGEEALDFLR--GEGEYadaprpDLILLDLNMPRMDGFEVLREIK--A 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1934323370 671 REDAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKL 719
Cdd:cd17557    77 DPDLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSL 125
PRK13557 PRK13557
histidine kinase; Provisional
497-680 3.42e-18

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 88.57  E-value: 3.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 497 IAVfqfvcSDTGLGMSEEFQKHAFDAF---AQEGKqstttfsGSGLGLSIVKDIVERMGGTIELESEENVGStfTVTVPF 573
Cdd:PRK13557  327 IAV-----TDTGSGMPPEILARVMDPFfttKEEGK-------GTGLGLSMVYGFAKQSGGAVRIYSEVGEGT--TVRLYF 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 574 EIDYLAENNDSQKDsySQDMDLSG-KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldEYDVIIMDV 652
Cdd:PRK13557  393 PASDQAENPEQEPK--ARAIDRGGtETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP--EVDLLFTDL 468
                         170       180
                  ....*....|....*....|....*....
gi 1934323370 653 MMP-VMDGLeatkairMLEREDAKKIPII 680
Cdd:PRK13557  469 IMPgGMNGV-------MLAREARRRQPKI 490
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
351-572 1.02e-17

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: 86.07  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 351 MSHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKKVLQSADYLQNLINNVLDIGKLESGSLVlehkSFDLAELLRNNLTV 430
Cdd:COG5806   208 IAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLE----KIDVSEELEHVIDV 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 431 vaMSAYENGVRFEggVEASTIRHRYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLG 510
Cdd:COG5806   284 --LSPYANMNNVE--IQTELEPGLYIEGDRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISI-----KDTGVG 354
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 511 MSEEfqkhafdAFAQEGKQ--STTTfSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG5806   355 MTKE-------QLERLGEPyfSTKE-KGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLP 410
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
600-707 4.99e-17

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: 77.17  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEatkAIRMLEREDAKK-IP 678
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEP---PDLILLDVMMPGMDGFE---VCRRLKADPATRhIP 74
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPI 707
Cdd:cd19920    75 VIFLTALTDTEDKVKGFELGAVDYITKPF 103
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
598-720 7.72e-17

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: 76.93  E-value: 7.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNIT-EAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:cd17542     1 KKVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPD---LVTMDITMPEMDGIEALKEI----KKIDPN 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17542    74 AKVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
598-720 8.77e-17

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: 76.96  E-value: 8.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRMLERedAKKI 677
Cdd:cd17562     1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKK---FDLIITDQNMPNMDGIELIKELRKLPA--YKFT 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17562    76 PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
465-572 1.34e-16

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: 75.99  E-value: 1.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 465 RVLMNLSSNAIKYNHFHGTVNVhCEELSDDGNiavFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIV 544
Cdd:cd16925     7 RVVLNLLSNAFKFTPDGGRIRC-ILEKFRLNR---FLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIV 82
                          90       100
                  ....*....|....*....|....*...
gi 1934323370 545 KDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16925    83 KEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
601-723 2.64e-16

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: 75.34  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 601 LLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPII 680
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEY---ALSGIYDLIILDIMLPGMDGLEVLKSL----REEGIETPVL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 681 AMTANAFEEDRKACLEAGMNEHIGKPIDIPRLkRAITKLLTKK 723
Cdd:cd17625    74 LLTALDAVEDRVKGLDLGADDYLPKPFSLAEL-LARIRALLRR 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
600-722 6.13e-16

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: 74.30  E-value: 6.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNIT---EAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:cd17536     1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHK---PDIVITDIRMPGMDGLELIEKI----RELYPD 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934323370 677 IPIIAMTANA-FEEDRKAcLEAGMNEHIGKPIDIPRLKRAITKLLTK 722
Cdd:cd17536    74 IKIIILSGYDdFEYAQKA-IRLGVVDYLLKPVDEEELEEALEKAKEE 119
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
329-572 8.38e-16

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.59  E-value: 8.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 329 QLKESMED--AHRANLSKTaflrrMSHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKKVLQSADYLQNLINNVLDIGKL 406
Cdd:PRK09835  250 HMIERIEDvfTRQSNFSAD-----IAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQA 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 407 ESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGV--RFEGgveastiRHRYLIGSPVHLSRVLMNLSSNAIKYNHFHGTV 484
Cdd:PRK09835  325 DNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVelRFVG-------DPCQVAGDPLMLRRAISNLLSNALRYTPAGEAI 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 485 NVHCEELSDdgniaVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEEnVG 564
Cdd:PRK09835  398 TVRCQEVDH-----QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RG 471

                  ....*...
gi 1934323370 565 STFTVTVP 572
Cdd:PRK09835  472 TRFVISLP 479
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
598-720 8.92e-16

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 74.12  E-value: 8.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEH-LNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRmlEREDAKK 676
Cdd:cd17552     2 KRILVIDDEEDIREVVQACLEKLAgWEVLTASSGQEGLEKAATEQPD---AILLDVMMPDMDGLATLKKLQ--ANPETQS 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17552    77 IPVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
352-572 1.15e-15

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 80.22  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 352 SHDIRTPLNGIVGMI-HIAEKYNNDVvKLRECRKKVLQSADYLQNLINNVLDIGKLESGSLvlehKSFDLAELLRNNLTV 430
Cdd:PRK10364  245 AHEIRNPLSSIKGLAkYFAERAPAGG-EAHQLAQVMAKEADRLNRVVSELLELVKPTHLAL----QAVDLNDLINHSLQL 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 431 VAMSAYENG--VRFEGGVEASTIRhryliGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTG 508
Cdd:PRK10364  320 VSQDANSREiqLRFTANDTLPEIQ-----ADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISV-----TDSG 389
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 509 LGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:PRK10364  390 KGIAADQLEAIFTPYF------TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLP 447
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
599-720 2.16e-15

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: 72.76  E-value: 2.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEE-EHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKI 677
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKElGFNNVEEAEDGVDALEKLKAG---GFDFVITDWNMPNMDGLELLKTIR--ADGALSHL 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd19923    77 PVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
600-721 3.45e-15

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


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 72.36  E-value: 3.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLdeyDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIPI 679
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRP---TLVISDIVMPEMDGYELCRKIK--SDPDLKDIPV 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLT 721
Cdd:cd17598    76 ILLTTLSDPRDVIRGLECGADNFITKPYDEKYLLSRIKYILV 117
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
599-712 4.76e-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: 71.66  E-value: 4.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQnSRLDEYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLA-SAEHSFQLVLLDLCMPEMDGFEVALRIR--KLFGRRERP 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 679 -IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd19933    79 lIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
600-706 4.99e-15

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: 71.32  E-value: 4.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNvinMEIAHAI---LEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:cd19935     1 ILVVEDE---KKLAEYLkkgLTEEGYAVDVAYDGEDGLHLALT---NEYDLIILDVMLPGLDGLEVLRRL----RAAGKQ 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd19935    71 TPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
600-720 5.26e-15

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: 71.77  E-value: 5.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEH-LNIT-EAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPdIEVVgEAADGEEALALLRELR---PDVVLMDLSMPGMDGIEALRRL----RRRYPDL 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17535    74 KVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAVA 116
envZ PRK09467
osmolarity sensor protein; Provisional
352-557 6.60e-15

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 77.64  E-value: 6.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 352 SHDIRTPLNGI---VGMI-----HIAEKYNNDVvklRECRKKVLQSADYLQNlinnvldiGKLESGSLVlehksfDLAEL 423
Cdd:PRK09467  237 SHDLRTPLTRIrlaTEMMseedgYLAESINKDI---EECNAIIEQFIDYLRT--------GQEMPMEMA------DLNAL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 424 LRNnlTVVAMSAYENGVRFEGGVEASTIRhryliGSPVHLSRVLMNLSSNAIKYNHfhGTVNVhceELSDDGNIAVFQFv 503
Cdd:PRK09467  300 LGE--VIAAESGYEREIETALQPGPIEVP-----MNPIAIKRALANLVVNAARYGN--GWIKV---SSGTEGKRAWFQV- 366
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 504 cSDTGLGMSEEFQKHAFDAFAQeGKQSTTTfSGSGLGLSIVKDIVERMGGTIEL 557
Cdd:PRK09467  367 -EDDGPGIPPEQLKHLFQPFTR-GDSARGS-SGTGLGLAIVKRIVDQHNGKVEL 417
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
601-712 2.01e-14

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: 69.99  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 601 LLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRMleREDAKKIPII 680
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKD---EKPDLIILDLMLPGIDGLEVCRILRS--DPKTSSIPII 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934323370 681 AMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd19937    76 MLTAKGEEFDKVLGLELGADDYITKPFSPREL 107
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
600-706 2.95e-14

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: 69.33  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRL------DEYDVIIMDVMMPVMDGLEATKAIrmleRED 673
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlsKELDLIITDIEMPKMDGYELTFEL----RDD 76
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 674 AK--KIPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd19924    77 PRlaNIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
599-722 3.34e-14

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: 69.73  E-value: 3.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDN-VINMEIAHAILEEEHLN-ITEAKNGKEAFEIFQnsRLDEyDVIIMDVMMPVMDGLEATKAIrMLERedakK 676
Cdd:cd17541     2 RVLIVDDSaVMRKLLSRILESDPDIEvVGTARDGEEALEKIK--ELKP-DVITLDIEMPVMDGLEALRRI-MAER----P 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKA--CLEAGMNEHIGKP--IDIPRLKRAITKLLTK 722
Cdd:cd17541    74 TPVVMVSSLTEEGAEITleALELGAVDFIAKPsgGISLDLEEIAEELIEK 123
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
460-572 3.63e-14

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: 68.99  E-value: 3.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 460 PVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAqegkqsTTTF--SGS 537
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEV-----EDTGSGIDPEILGRIFDPFF------TTKPvgEGT 69
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16943    70 GLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-571 5.10e-14

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: 69.08  E-value: 5.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHFHGTVNVHCEElsDDGNIAVfqfVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLS 542
Cdd:cd16947    21 LQRILKNLISNAIKYGSDGKFLGMTLRE--DEKHVYI---DIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLT 95
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTVTV 571
Cdd:cd16947    96 ITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
598-706 6.70e-14

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: 68.43  E-value: 6.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKI 677
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPR---PDLILLDWMLPGGSGIQFIRRLK--RDEMTRDI 75
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17618    76 PIIMLTARGEEEDKVRGLEAGADDYITKP 104
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 7.83e-14

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: 67.81  E-value: 7.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKynhfhGTVNVHCE--EL------SDDGNIAVFqfVCsDTGLGMSEEFQKHAFDAFAqegkqsTTTF 534
Cdd:cd16920     1 IQQVLINLVRNGIE-----AMSEGGCErrELtirtspADDRAVTIS--VK-DTGPGIAEEVAGQLFDPFY------TTKS 66
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1934323370 535 SGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16920    67 EGLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
599-720 9.12e-14

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 74.11  E-value: 9.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLV--EDNVINMeiAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLERedakK 676
Cdd:PRK11361    6 RILIVddEDNVRRM--LSTAFALQGFETHCANNGRTALHLFADIHPD---VVLMDIRMPEMDGIKALKEMRSHET----R 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK11361   77 TPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRAL 120
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
597-716 1.21e-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: 69.99  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 597 GKRVLLVEDNVINMEIAHAILEEE-HLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAK 675
Cdd:COG3707     3 GLRVLVVDDEPLRRADLREGLREAgYEVVAEAADGEDAVEL---VRELKPDLVIVDIDMPDRDGLEAARQIS-----EER 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:COG3707    75 PAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
352-716 2.19e-13

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 73.94  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 352 SHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKKVLQSADYLQNLINNVLDIGKLESGSLvlehKSFDLAELLRNNLTVV 431
Cdd:PRK13837  458 AHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGRKGERNT----KPFDLSELVTEIAPLL 533
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 432 AMSAYEnGVRFEggVEASTIRHRYLiGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCE--------ELSDdGNIAVFQFV 503
Cdd:PRK13837  534 RVSLPP-GVELD--FDQDQEPAVVE-GNPAELQQVLMNLCSNAAQAMDGAGRVDISLSraklrapkVLSH-GVLPPGRYV 608
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 504 ---CSDTGLGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPfEIDYLAE 580
Cdd:PRK13837  609 llrVSDTGAGIDEAVLPHIFEPFF------TTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLP-PSSKVPV 681
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 581 NNDSQKDSYSQDMDlSGKRVLLVE-DNVINM---EIAHAI---------LEEEhlnITEAKNGKEAFE--IFQNSRLDEY 645
Cdd:PRK13837  682 APQAFFGPGPLPRG-RGETVLLVEpDDATLEryeEKLAALgyepvgfstLAAA---IAWISKGPERFDlvLVDDRLLDEE 757
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 646 DVIImdvmmpvmdgleatkAIRMLeredAKKIPIIaMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:PRK13837  758 QAAA---------------ALHAA----APTLPII-LGGNSKTMALSPDLLASVAEILAKPISSRTLAYAL 808
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
501-572 2.42e-13

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: 67.02  E-value: 2.42e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934323370 501 QFVC---SDTGLGMSEEFQKHAFDAF---AQEGKqstttfsGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16919    46 NYVClevSDTGSGMPAEVLRRAFEPFfttKEVGK-------GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-569 2.43e-13

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: 66.72  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHFHGTVNVHCEelsDDGNIavFQFVCSDTGLGMSEEFQKHAFDAFAQeGKQSTTTFSGSGLGLS 542
Cdd:cd16975     5 LSRALINIISNACQYAPEGGTVSISIY---DEEEY--LYFEIWDNGHGFSEQDLKKALELFYR-DDTSRRSGGHYGMGLY 78
                          90       100
                  ....*....|....*....|....*..
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTV 569
Cdd:cd16975    79 IAKNLVEKHGGSLIIENSQKGGAEVTV 105
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
343-409 4.49e-13

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 64.54  E-value: 4.49e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934323370 343 SKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDvVKLRECRKKVLQSADYLQNLINNVLDIGKLESG 409
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLD-EEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
486-572 5.31e-13

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: 65.39  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 486 VHCEeLSDDGNIAVFqfVCSDTGLGMSEEFQKHAFdafaQEGkQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGS 565
Cdd:cd16915    26 VEVF-LRDEGDDLVI--EVRDTGPGIAPELRDKVF----ERG-VSTKGQGERGIGLALVRQSVERLGGSITVESEPGGGT 97

                  ....*..
gi 1934323370 566 TFTVTVP 572
Cdd:cd16915    98 TFSIRIP 104
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
600-720 5.56e-13

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: 65.87  E-value: 5.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIrmleREDAKKIPI 679
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPD---AVVLDVMMPRLDGLEVCRRL----RAAGNDLPI 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17627    74 LVLTARDSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
600-712 6.28e-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: 65.58  E-value: 6.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVInmeIAHAI---LEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:cd17624     1 ILLVEDDAL---LGDGLktgLRKAGYAVDWVRTGAEAEAALASG---PYDLVILDLGLPDGDGLDLLRRW----RRQGQS 70
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd17624    71 LPVLILTARDGVDDRVAGLDAGADDYLVKPFALEEL 106
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
458-573 6.64e-13

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: 65.50  E-value: 6.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEElSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGKQSTTtfsGS 537
Cdd:cd16940     9 GDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSA-DDGAVIRV-----EDNGPGIDEEELEALFERFYRSDGQNYG---GS 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 538 GLGLSIVKDIVERMGGTIELesEENVGSTFTVTVPF 573
Cdd:cd16940    80 GLGLSIVKRIVELHGGQIFL--GNAQGGGLEAWVRL 113
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
598-716 1.10e-12

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 65.13  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDN-VINMEIAHAILEEEHLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKK 676
Cdd:cd19932     1 VRVLIAEDEaLIRMDLREMLEEAGYEVVGEASDGEEAVEL---AKKHKPDLVIMDVKMPRLDGIEAAKIIT-----SENI 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:cd19932    73 APIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
598-684 1.88e-12

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 64.16  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd17554     1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED---PDLVILDIKMPGMDGLETLRKI----REKKPDL 73

                  ....*..
gi 1934323370 678 PIIAMTA 684
Cdd:cd17554    74 PVIICTA 80
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
600-711 2.02e-12

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: 64.25  E-value: 2.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFeifQNSRLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKKIPI 679
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGL---AALLEGSPDLVVLDVMLPKMNGLDVLKELR-----KTSQVPV 72
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:cd17623    73 LMLTARGDDIDRILGLELGADDYLPKPFN-PR 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
598-655 2.14e-12

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 62.20  E-value: 2.14e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1934323370  598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMP 655
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE---EKPDLILLDIMMP 55
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
271-572 3.96e-12

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 68.99  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 271 ERLRNTNSVSIEFMGVNGEWRLAR-FIVKSRDAHGNAVDVLYVVRDITEeksrelmyQKQLKESMedahrANLSKTAFLR 349
Cdd:COG5805   222 TEVWQEFIIEREIITKDGRIRYFEaVIVPLIDTDGSVKGILVILRDITE--------KKEAEELM-----ARSEKLSIAG 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 350 RMS----HDIRTPLNGIVGMIHI--AEKynndvvklrECRKK----VLQSADYLQNLINNVLDIGKLESGSLvlehKSFD 419
Cdd:COG5805   289 QLAagiaHEIRNPLTSIKGFLQLlqPGI---------EDKEEyfdiMLSELDRIESIISEFLALAKPQAVNK----EKEN 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 420 LAELLRNNLTVVAMSAYENGVRFEGGVEASTIrhrYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAV 499
Cdd:COG5805   356 INELIQDVVTLLETEAILHNIQIRLELLDEDP---FIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRV 432
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 500 fqfvcSDTGLGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:COG5805   433 -----IDEGIGIPEERLKKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
599-723 6.19e-12

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 65.99  E-value: 6.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEE-EHLNI-TEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKK 676
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKyPDLEVvGEASNGEEALELLEEHK---PDLVFLDIQMPGLDGFELARQL----RELDPP 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 677 IPIIAMTA------NAFEEDrkACleagmnEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG3279    76 PPIIFTTAydeyalEAFEVN--AV------DYLLKPIDEERLAKALEKAKERL 120
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
599-720 7.04e-12

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: 62.78  E-value: 7.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKKIP 678
Cdd:cd17622     2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAR---EKPDAVLLDIMLPGIDGLTLCRDLR-----PKYQGP 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17622    74 ILLLTALDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
393-572 7.23e-12

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 68.33  E-value: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 393 LQNLINNVLDIGKLESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIRhryliGSPVHLSRVLMNLSS 472
Cdd:PRK11100  304 LQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRPDDARVL-----GDPFLLRQALGNLLD 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 473 NAIKYNHFHGTVNVHCEELSDDGNIAVFqfvcsDTGLGMSEEFQKHAFDAF-----AQEGKQSTttfsgsGLGLSIVKDI 547
Cdd:PRK11100  379 NAIDFSPEGGTITLSAEVDGEQVALSVE-----DQGPGIPDYALPRIFERFyslprPANGRKST------GLGLAFVREV 447
                         170       180
                  ....*....|....*....|....*
gi 1934323370 548 VERMGGTIELESEENVGSTFTVTVP 572
Cdd:PRK11100  448 ARLHGGEVTLRNRPEGGVLATLTLP 472
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
599-712 9.70e-12

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: 62.37  E-value: 9.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIrmleREDAKKIP 678
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPD---AVVLDIMLPDMDGLEVLRRL----RADGPDVP 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd17615    74 VLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
GAF COG2203
GAF domain [Signal transduction mechanisms];
19-274 9.96e-12

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 68.30  E-value: 9.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  19 TILHQISlmDQVENEQELSEIIHSLLQAIGNYTGADRVYVFDWETDQkdslsNTFEWCAdGVAPEIDNLQAIPVSSMPnW 98
Cdd:COG2203   193 ALLNEIS--QALRSALDLEELLQRILELAGELLGADRGAILLVDEDG-----GELELVA-APGLPEEELGRLPLGEGL-A 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  99 VKRFENKEVIVIHDLEATKNSEPEEYELLKTQEICSLIAVPIYANHQMNGFIGVDNPDLRQ-NEISITLLSDVGGHLGCV 177
Cdd:COG2203   264 GRALRTGEPVVVNDASTDPRFAPSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAfTEEDLELLEALADQAAIA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 178 RENLKSTVLLKKALDEATKRSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEER 257
Cdd:COG2203   344 IERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLL 423
                         250
                  ....*....|....*..
gi 1934323370 258 EKYREFLDFDTLTERLR 274
Cdd:COG2203   424 LDLLLLLLLLRRILLLR 440
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
460-572 1.41e-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: 61.71  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 460 PVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDdgniaVFQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGL 539
Cdd:cd16946     2 RDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQ-----EVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 540 GLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16946    77 GLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
599-706 1.82e-11

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 61.72  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRmlereDAKKIP 678
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPD---LVLLDLMLPGIDGIEVCRQIR-----AESGVP 73
                          90       100
                  ....*....|....*....|....*...
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17626    74 IVMLTAKSDTVDVVLGLESGADDYVAKP 101
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
343-409 2.07e-11

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 59.89  E-value: 2.07e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934323370  343 SKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDvVKLRECRKKVLQSADYLQNLINNVLDIGKLESG 409
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELS-EEQREYLETILREAERLLRLINDLLDLSRIEAG 66
PRK11517 PRK11517
DNA-binding response regulator HprR;
599-712 2.52e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 64.15  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMPVMDGLEATKAIRMleredAKKIP 678
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYL---ALKDDYALIILDIMLPGMDGWQILQTLRT-----AKQTP 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:PRK11517   74 VICLTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-564 3.57e-11

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: 60.16  E-value: 3.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHfhGTVNVHCEelsDDGNIAVFQFVcsDTGLGMSEEFQKHAFDAFAQeGKQSTTTfSGSGLGLS 542
Cdd:cd16950     1 LKRVLSNLVDNALRYGG--GWVEVSSD---GEGNRTRIQVL--DNGPGIAPEEVDELFQPFYR-GDNARGT-SGTGLGLA 71
                          90       100
                  ....*....|....*....|..
gi 1934323370 543 IVKDIVERMGGTIELESEENVG 564
Cdd:cd16950    72 IVQRISDAHGGSLTLANRAGGG 93
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 3.91e-11

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 60.14  E-value: 3.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHfhGTVNVhceELSDDGNIAVFQfvCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLS 542
Cdd:cd16939     1 MARALDNLLRNALRYAH--RTVRI---ALLVSGGRLTLI--VEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLA 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16939    74 IVHRVALWHGGHVECDDSELGGACFRLTWP 103
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
600-706 5.05e-11

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: 59.70  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIfqnsrLDEY--DVIIMDVMMPVMDGLEATKAIRmlEREDAKKI 677
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDL-----LNQYipDLIISDIIMPGVDGYSLLGKLR--KNADFDTI 73
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd19927    74 PVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
pleD PRK09581
response regulator PleD; Reviewed
599-713 6.54e-11

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 65.31  E-value: 6.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICER---EQPDIILLDVMMPGMDGFEVCRRLK--SDPATTHIP 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPID----IPRLK 713
Cdd:PRK09581   79 VVMVTALDDPEDRVRGLEAGADDFLTKPINdvalFARVK 117
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
341-405 6.89e-11

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: 58.38  E-value: 6.89e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934323370 341 NLSKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKKVLQSADYLQNLINNVLDIGK 405
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
599-711 9.64e-11

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: 59.32  E-value: 9.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLdeyDVIIMDVMMPVMDGLEATKAIRmlereDAKKIP 678
Cdd:cd17619     2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI---DLVLLDINLPGKDGLSLTRELR-----EQSEVG 73
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:cd17619    74 IILVTGRDDEVDRIVGLEIGADDYVTKPFN-PR 105
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
600-706 1.03e-10

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: 59.60  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVInmeIAHAI---LEEEHLNITEAKNGKEAFeiFQNSRlDEYDVIIMDVMMPVMDGLEatkAIRMLeREDAKK 676
Cdd:cd19934     1 LLLVEDDAL---LAAQLkeqLSDAGYVVDVAEDGEEAL--FQGEE-EPYDLVVLDLGLPGMDGLS---VLRRW-RSEGRA 70
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd19934    71 TPVLILTARDSWQDKVEGLDAGADDYLTKP 100
PRK09303 PRK09303
histidine kinase;
466-572 1.04e-10

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 64.20  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 466 VLMNLSSNAIKYNHFHGTVNvhceelsddgnIAVF-------QFVCSDTGLGMSEEFQKHAF-DAFAQegKQSTTTfSGS 537
Cdd:PRK09303  276 VLLNLLDNAIKYTPEGGTIT-----------LSMLhrttqkvQVSICDTGPGIPEEEQERIFeDRVRL--PRDEGT-EGY 341
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 538 GLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:PRK09303  342 GIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
598-716 1.05e-10

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: 59.34  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVIN-MEIAhAILEEEHLNITE-AKNGKEAFEIFQNSRLdeyDVIIMDVMMP-VMDGLEATKAIRmlereDA 674
Cdd:cd17534     1 KKILIVEDEAIIaLDLK-EILESLGYEVVGiADSGEEAIELAEENKP---DLILMDINLKgDMDGIEAAREIR-----EK 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 675 KKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAI 716
Cdd:cd17534    72 FDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
PRK10610 PRK10610
chemotaxis protein CheY;
599-724 1.08e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 59.99  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHL-NITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIrmleREDAK-- 675
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALNKLQAG---GFGFVISDWNMPNMDGLELLKTI----RADGAms 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTKKG 724
Cdd:PRK10610   80 ALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLG 128
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
599-711 1.48e-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: 58.93  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIRmlereDAKKIP 678
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHT---PPDLILLDLMLPGTDGLTLCREIR-----RFSDVP 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:cd19938    73 IIMVTARVEEIDRLLGLELGADDYICKPYS-PR 104
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
599-708 1.49e-10

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 61.74  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldeYDVIIMDVMMPVMDGLEATKAIRMleredAKKIP 678
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDS----IDLLLLDVMMPKKNGIDTLKELRQ-----THQTP 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPID 708
Cdd:PRK10955   74 VIMLTARGSELDRVLGLELGADDYLPKPFN 103
PRK10604 PRK10604
sensor protein RstB; Provisional
343-572 1.83e-10

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 63.47  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 343 SKTAFLRRMSHDIRTPLngivgmihiaekynndvVKLREcRKKVLQ--SAD----------YLQNLINNVLDIGKLESGS 410
Cdd:PRK10604  211 SKKQLIDGIAHELRTPL-----------------VRLRY-RLEMSDnlSAAesqalnrdigQLEALIEELLTYARLDRPQ 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 411 LVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEAStirhrYLIGSPVHLSRVLMNLSSNAIKYNHfhGTVNVHcee 490
Cdd:PRK10604  273 NELHLSEPDLPAWLSTHLADIQAVTPEKTVRLDTPHQGD-----YGALDMRLMERVLDNLLNNALRYAH--SRVRVS--- 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 491 LSDDGNIAVFQFvcSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVT 570
Cdd:PRK10604  343 LLLDGNQACLIV--EDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFS 420

                  ..
gi 1934323370 571 VP 572
Cdd:PRK10604  421 WP 422
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
600-720 2.34e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 63.51  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEifqNSRLDEYDVIIMDVMMPVMDGLEATKAIRMLEredaKKIPI 679
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALE---QVREQVFDLVLCDVRMAEMDGIATLKEIKALN----PAIPV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK10365   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
600-706 2.42e-10

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: 58.20  E-value: 2.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQnsrLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKKIPI 679
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVE---EEQPDLILLDLMLPEKDGLEVCREVR-----KTSNVPI 72
                          90       100
                  ....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17614    73 IMLTAKDSEVDKVLGLELGADDYVTKP 99
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
599-706 2.78e-10

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: 58.30  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldEYDVIIMDVMMPVMDGLEATKAIRmlEREDAKKIP 678
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHP--DIKLVITDYNMPEMDGFELVREIR--KKYSRDQLA 77
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 679 II--------AMTANaFeedrkacLEAGMNEHIGKP 706
Cdd:cd17544    78 IIgisasgdnALSAR-F-------IKAGANDFLTKP 105
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
599-712 3.93e-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: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFqnsRLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKKIP 678
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRI---IDEQPSLVVLDIMLPGMDGLTVCREVR-----EHSHVP 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDiPRL 712
Cdd:cd19939    73 ILMLTARTEEMDRVLGLEMGADDYLCKPFS-PRE 105
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
600-713 4.81e-10

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


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 57.64  E-value: 4.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRlDEYDVIIMDVMMPVMDGLEATKAIRMLeredaKKIPI 679
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENK-DEFDLVITDVHMPDMDGFEFLELIRLE-----MDLPV 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLK 713
Cdd:cd17584    75 IMMSADGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
505-574 5.82e-10

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 62.24  E-value: 5.82e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 505 SDTGLGMSEEFQKHAFDafaqegKQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:PRK11086  473 SDDGPGIAPDEIDAIFD------KGYSTKGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWD 536
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 6.59e-10

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: 56.91  E-value: 6.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHFHGTVNVHCEElsDDGNIavfQFVCSDTGLGMSEEFQKHAFDAF--AQEGKQSTTTfsgSGLG 540
Cdd:cd16948     6 LSFIIGQIVSNALKYSKQGGKIEIYSET--NEQGV---VLSIKDFGIGIPEEDLPRVFDKGftGENGRNFQES---TGMG 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934323370 541 LSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16948    78 LYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
599-723 9.69e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 60.93  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDN-VINMEIAhAILEEEHlNIT---EAKNGKEAFEifQNSRLDEyDVIIMDVMMPVMDGLEATKAIrMLEReda 674
Cdd:PRK00742    5 RVLVVDDSaFMRRLIS-EILNSDP-DIEvvgTAPDGLEARE--KIKKLNP-DVITLDVEMPVMDGLDALEKI-MRLR--- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 675 kKIPII---AMTANAFEEDRKAcLEAGMNEHIGKP-IDIPRLKRAITKLLTKK 723
Cdd:PRK00742   76 -PTPVVmvsSLTERGAEITLRA-LELGAVDFVTKPfLGISLGMDEYKEELAEK 126
ompR PRK09468
osmolarity response regulator; Provisional
593-711 2.25e-09

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 58.45  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKeafeifQNSRL---DEYDVIIMDVMMPVMDGLEATKaiRMl 669
Cdd:PRK09468    1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAE------QMDRLltrESFHLMVLDLMLPGEDGLSICR--RL- 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 670 eREDAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:PRK09468   72 -RSQNNPTPIIMLTAKGEEVDRIVGLEIGADDYLPKPFN-PR 111
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 2.26e-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: 55.29  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLS 542
Cdd:cd16952     1 LRSAFSNLVSNAVKYTPPSDTITVRWSQEESGARLSV-----EDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLA 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16952    76 IVKHVMSRHDARLLIASELGKGSRFTCLFP 105
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
598-707 2.52e-09

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 55.28  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFqnsRLDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd17555     1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELF---RSEQPDLVLCDLRMPEMDGLEVLKQI----TKESPDT 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPI 707
Cdd:cd17555    74 PVIVVSGAGVMSDAVEALRLGAWDYLTKPI 103
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
598-719 2.91e-09

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: 55.24  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVED-NVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLdeyDVIIMDVMMPVMDGLEATKAIRMLEREdakk 676
Cdd:cd17593     1 MKVLICDDsSMARKQLARALPADWDVEITFAENGEEALEILREGRI---DVLFLDLTMPVMDGYEVLEALPVEQLE---- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKL 719
Cdd:cd17593    74 TKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
528-572 2.98e-09

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 56.82  E-value: 2.98e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1934323370 528 KQSTTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16916   134 AEQVTDVSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
PRK10337 PRK10337
sensor protein QseC; Provisional
353-571 3.74e-09

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 59.66  E-value: 3.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 353 HDIRTPLNgivgmihiAEKYNNDVVKLR----ECRKKVL----QSADYLQNLINNVLDIGKLESGSLVLEHKSFDLAELL 424
Cdd:PRK10337  246 HELRSPLA--------ALKVQTEVAQLSdddpQARKKALlqlhAGIDRATRLVDQLLTLSRLDSLDNLQDVAEIPLEDLL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 425 RNnlTVVAM--SAYENGVRFEGGVEASTIRHRyliGSPVHLSRVLMNLSSNAIKYNHFHGTVNVhceELSDDGniavfqF 502
Cdd:PRK10337  318 QS--AVMDIyhTAQQAGIDVRLTLNAHPVIRT---GQPLLLSLLVRNLLDNAIRYSPQGSVVDV---TLNARN------F 383
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934323370 503 VCSDTGLGMSEEFQKHAFDAFAQEGKQSTTtfsGSGLGLSIVKDIVERMGGTIELESEENVGstFTVTV 571
Cdd:PRK10337  384 TVRDNGPGVTPEALARIGERFYRPPGQEAT---GSGLGLSIVRRIAKLHGMNVSFGNAPEGG--FEAKV 447
orf27 CHL00148
Ycf27; Reviewed
593-720 4.11e-09

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 57.80  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFqnsRLDEYDVIIMDVMMPVMDGLEATKAIRmlere 672
Cdd:CHL00148    2 MENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLF---RKEQPDLVILDVMMPKLDGYGVCQEIR----- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1934323370 673 DAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:CHL00148   74 KESDVPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
600-706 4.46e-09

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: 54.09  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVinmEIAHAI---LEEEHLNITEAKNGKEAFeifQNSRLDEYDVIIMDVMMPVMDGLEATKAIRmlereDAKK 676
Cdd:cd17620     1 ILVIEDEP---QIRRFLrtaLEAHGYRVFEAETGQEGL---LEAATRKPDLIILDLGLPDMDGLEVIRRLR-----EWSA 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17620    70 VPVIVLSARDEESDKIAALDAGADDYLTKP 99
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-569 5.02e-09

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


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 54.39  E-value: 5.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHF--HGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAF---AQEGKqstttfsGS 537
Cdd:cd16976     1 IQQVLMNLLQNALDAMGKveNPRIRIAARRLGGRLVLVV-----RDNGPGIAEEHLSRVFDPFfttKPVGK-------GT 68
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1934323370 538 GLGLSIVKDIVERMGGTIELESEENVGSTFTV 569
Cdd:cd16976    69 GLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
617-716 5.85e-09

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: 54.59  E-value: 5.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 617 LEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIrmleREDAKKIPIIAMTANAFEEDRKACLE 696
Cdd:cd19919    20 LAGAGLTVTSFENAQEALAALASSQPD---VLISDIRMPGMDGLALLAQI----KQRHPDLPVIIMTAHSDLDSAVSAYQ 92
                          90       100
                  ....*....|....*....|....
gi 1934323370 697 AGMNEHIGKPIDIPR----LKRAI 716
Cdd:cd19919    93 GGAFEYLPKPFDIDEavalVERAI 116
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
599-666 7.14e-09

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 54.51  E-value: 7.14e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDN-VINMEIAHAILEEEHLN-ITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAI 666
Cdd:COG2197     3 RVLIVDDHpLVREGLRALLEAEPDIEvVGEAADGEEALELLEELRPD---VVLLDIRMPGMDGLEALRRL 69
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
600-712 7.18e-09

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: 54.29  E-value: 7.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIF------QNSRLDEYDV--IIMDVMMPVMDGLEATKAIRmlER 671
Cdd:cd17581     1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeeDSSNFNEPKVnmIITDYCMPGMTGYDLLKKVK--ES 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 672 EDAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPI---DIPRL 712
Cdd:cd17581    79 SALKEIPVVIMSSENIPTRISRCLEEGAEDFLLKPVklaDVKRL 122
Spo0A COG5801
Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell ...
599-723 8.83e-09

Stage 0 sporulation initiation regulator Spo0A (response regulator, REC-HTH domains) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444503 [Multi-domain]  Cd Length: 264  Bit Score: 57.12  E-value: 8.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVinmEIAHAIleEEHLN-------ITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIRMLER 671
Cdd:COG5801     6 KVLIADDNR---EFCELL--EEYLSsqpdmevVGVAYNGLEALELIEEK---KPDVVILDIIMPHLDGLGVLEKLREMNL 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1934323370 672 EdaKKIPIIAMTanAFEED---RKAcLEAGMNEHIGKPIDIPRLKRAITKLLTKK 723
Cdd:COG5801    78 E--KRPKVIMLT--AFGQEditQRA-VELGADYYILKPFDLDVLAERIRQLAGGK 127
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 9.27e-09

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: 53.54  E-value: 9.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNhFHGTVnVHCEELSDDGNIAVfqfVCSDTGLGMSEEFQKHAFDAFAQeGKQSTTTfSGSGLGLS 542
Cdd:cd16923     1 LQRVFSNLLSNAIKYS-PENTR-IYITSFLTDDVVNI---MFKNPSSHPLDFKLEKLFERFYR-GDNSRNT-EGAGLGLS 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 543 IVKDIVERMGGTIELESEENvGSTFTVTVP 572
Cdd:cd16923    74 IAKAIIELHGGSASAEYDDN-HDLFKVRLP 102
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
600-720 1.08e-08

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: 53.74  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPI 679
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP---PDVVLLDLKLPDMSGMEILKWI----QERSLPTSV 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1934323370 680 IAMTAN-----AFEEDRKacleaGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17572    74 IVITAHgsvdiAVEAMRL-----GAYDFLEKPFDADRLRVTVRNAL 114
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 1.36e-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: 53.10  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYNHfhGTVNVHCEElsDDGNIavfQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLS 542
Cdd:cd16949     1 LARALENVLRNALRYSP--SKILLDISQ--DGDQW---TITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLA 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16949    74 IAERAIEQHGGKIKASNRKPGGLRVRIWLP 103
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
183-574 1.49e-08

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 57.99  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 183 STVLLKKALDEATKRSEIIAAIATLYVTIVQANVKERTYELLKGHDLVQKILGQKGKIDDVMERLPTAFAAQEEREKYRE 262
Cdd:COG3920   145 ALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALLL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 263 FLDFDTLTERLRNTNSVSIEFMGVNGEWRLARFIVKSRDAHGNAVDVLYVVRDITEEKSRELMYQKQLKEsmedahranl 342
Cdd:COG3920   225 VLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEE---------- 294
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 343 sKTAFLRRMSHDIRTPLNGIVGMIHI-AEKYNNDVVK--LRECRKKVLQSAdylqnLINNVLdigkLESGSLvlehKSFD 419
Cdd:COG3920   295 -KELLLRELHHRVKNNLQVVSSLLRLqARRADDPEAReaLEESQNRIQALA-----LVHELL----YQSEDW----EGVD 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 420 LAELLRNNLTVVAMSAYENGVRFEggveastirhryLIGSPVHLSR-------VLMN-LSSNAIKY---NHFHGTVNVHC 488
Cdd:COG3920   361 LRDYLRELLEPLRDSYGGRGIRIE------------LDGPDVELPAdaavplgLILNeLVTNALKHaflSGEGGRIRVSW 428
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 489 EElsDDGNiavFQFVCSDTGLGMSEEFQKHafdafaqegkqstttfSGSGLGLSIVKDIVERMGGTIELESEEnvGSTFT 568
Cdd:COG3920   429 RR--EDGR---LRLTVSDNGVGLPEDVDPP----------------ARKGLGLRLIRALVRQLGGTLELDRPE--GTRVR 485

                  ....*.
gi 1934323370 569 VTVPFE 574
Cdd:COG3920   486 ITFPLA 491
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
343-576 1.64e-08

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 57.72  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 343 SKTAFLRRMSHDIRTPLNGIVGMIhiaEKYNNDVvklrecRKKVLQSADYLQ----NLINNVLDIGKL---ESGSLVLEH 415
Cdd:PRK10549  239 MRRDFMADISHELRTPLAVLRGEL---EAIQDGV------RKFTPESVASLQaevgTLTKLVDDLHQLslsDEGALAYRK 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 416 KSFDLAELLRnnltvVAMSAYENgvRFEG---GVEASTIRHRYLIGSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEeLS 492
Cdd:PRK10549  310 TPVDLVPLLE-----VAGGAFRE--RFASrglTLQLSLPDSATVFGDPDRLMQLFNNLLENSLRYTDSGGSLHISAE-QR 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 493 DDGNIAVFQfvcsDTGLGMSEEFQKHAFDAFAQ-EGKQSTTTfSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTV 571
Cdd:PRK10549  382 DKTLRLTFA----DSAPGVSDEQLQKLFERFYRtEGSRNRAS-GGSGLGLAICLNIVEAHNGRIIAAHSPFGGVSITVEL 456

                  ....*
gi 1934323370 572 PFEID 576
Cdd:PRK10549  457 PLERD 461
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
600-716 2.56e-08

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 52.50  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPI 679
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERR---PDLVLLDIWLPDMDGLELLKEI----KEKYPDLPV 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL----KRAI 716
Cdd:cd17550    74 IMISGHGTIETAVKATKLGAYDFIEKPLSLDRLlltiERAL 114
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
530-573 2.77e-08

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 57.11  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1934323370 530 ST----TTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPF 573
Cdd:COG0643   371 STaeevTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
597-719 3.18e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 55.11  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 597 GKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFeifqnSRLDEY--DVIIMDVMMPVMDGLEAtkaIRMLERED- 673
Cdd:PRK10161    2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAV-----NQLNEPwpDLILLDWMLPGGSGIQF---IKHLKRESm 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1934323370 674 AKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPID----IPRLKRAITKL 719
Cdd:PRK10161   74 TRDIPVVMLTARGEEEDRVRGLETGADDYITKPFSpkelVARIKAVMRRI 123
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
594-720 5.91e-08

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 51.79  E-value: 5.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 594 DLSGKRVLLVEdnvinmeiahaILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLEREd 673
Cdd:cd17553     8 DQYGIRILLNE-----------VFNKEGYQTFQAANGLQALDIVTKERPD---LVLLDMKIPGMDGIEILKRMKVIDEN- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934323370 674 akkIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:cd17553    73 ---IRVIIMTAYGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
35-175 7.43e-08

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 51.71  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370  35 ELSEIIHSLLQAIGNYTGADRVYVFDWETDQKDSLSNTFEW--CADGVAPEIDNLQAipvssmpnwvkrFENKEVIVIHD 112
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWlkAAGLEIPPGTGVTV------------LRTGRPLVVPD 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 113 LEATkNSEPEEYELLKTQEICSLIAVPIYANHQMNGFIGVDNPDLRQNEISITLLSDVGGHLG 175
Cdd:pfam01590  69 AAGD-PRFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPRPPFTEEELELLEVLADQVA 130
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
310-572 9.09e-08

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 55.02  E-value: 9.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 310 LYVVRDITEeksrelmyQKQLkesmEDAHRAnlsktaFLRRMSHDIRTPLNGIVGMIHIAEkynnDVVKLRECRKKVLQS 389
Cdd:PRK11006  188 LMVARDVTQ--------MHQL----EGARRN------FFANVSHELRTPLTVLQGYLEMMQ----DQPLEGALREKALHT 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 390 ----ADYLQNLINNVLDIGKLESGSLVLEHKSFDLAELLRN-NLTVVAMSAYENGVRFEggVEASTirhrYLIGSPVHLS 464
Cdd:PRK11006  246 mreqTQRMEGLVKQLLTLSKIEAAPTIDLNEKVDVPMMLRVlEREAQTLSQGKHTITFE--VDNSL----KVFGNEDQLR 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 465 RVLMNLSSNAIKYNHFHGTVNVhCEELSDDGNiavfQFVCSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGLSIV 544
Cdd:PRK11006  320 SAISNLVYNAVNHTPEGTHITV-RWQRVPQGA----EFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIV 394
                         250       260
                  ....*....|....*....|....*...
gi 1934323370 545 KDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:PRK11006  395 KHALSHHDSRLEIESEVGKGTRFSFVLP 422
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
599-686 1.29e-07

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


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 50.19  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVED-NVINMEIAHAiLEEEHLNITEAKNGKEAFEIFQNSRldEYDVIIMDVMMPVMDGLEatkaIRMLEREDAKKI 677
Cdd:cd18160     1 TILLADDePSVRKFIVTT-LKKAGYAVTEAESGAEALEKLQQGK--DIDIVVTDIVMPEMDGIE----LAREARKIDPDV 73

                  ....*....
gi 1934323370 678 PIIAMTANA 686
Cdd:cd18160    74 KILFISGGA 82
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
598-720 1.54e-07

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


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 50.48  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 598 KRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEatkairMLERedAKKI 677
Cdd:cd17569     1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQ---EPVDVVISDQRMPGMDGAE------LLKR--VRER 69
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1934323370 678 ---PI-IAMTANAfeeDRKACLEAgMNE-----HIGKPIDIPRLKRAITKLL 720
Cdd:cd17569    70 ypdTVrILLTGYA---DLDAAIEA-INEgeiyrFLTKPWDDEELKETIRQAL 117
PRK15479 PRK15479
transcriptional regulator TctD;
599-720 1.74e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 52.42  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNvinMEIAHAI---LEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAK 675
Cdd:PRK15479    2 RLLLAEDN---RELAHWLekaLVQNGFAVDCVFDGLAADHLLQS---EMYALAVLDINMPGMDGLEVLQRL----RKRGQ 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK15479   72 TLPVLLLTARSAVADRVKGLNVGADDYLPKPFELEELDARLRALL 116
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
600-706 2.34e-07

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: 49.50  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMleredAKKIPI 679
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGAD---IVLLDLMLPGLSGTEVCRQLRA-----RSNVPV 72
                          90       100
                  ....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17621    73 IMVTAKDSEIDKVVGLELGADDYVTKP 99
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
600-712 2.41e-07

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: 49.75  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLdeyDVIIMDVMMPVMDGLEatkAIRMLEREDAkkIPI 679
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRV---DLVLLDLRLGQESGLD---LLRTIRARSD--VPI 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 680 IAMTANAFEE-DRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd17594    74 IIISGDRRDEiDRVVGLELGADDYLAKPFGLREL 107
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
310-576 2.83e-07

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 54.17  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 310 LYVVRDiteeKSRELMYQKQLKEsmedAHR---ANL-SKTAFLRRMSHDIRTPLNGIVGMIHIAEKYNNDVVKLRECRKk 385
Cdd:PRK10618  420 LFLLRD----QDREVLVNKKLQQ----AQReyeKNQqARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQ- 490
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 386 VLQSADYLQNLINNVLDIGKLESGSLVLEHKSFDLAELLRNNLTVVAMSAYENGVRFEGGVEASTIRHRylIGSPVHLSR 465
Cdd:PRK10618  491 LAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLR--IGDRDALRK 568
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 466 VLMNLSSNAIKYNHFhGTVNVHCEelSDDGNIAVFQFVCSDTGLGMSEEFQ---KHAFDAFAQEGKQStttfSGSGLGLS 542
Cdd:PRK10618  569 ILLLLLNYAITTTAY-GKITLEVD--QDESSPDRLTIRILDTGAGVSIKELdnlHFPFLNQTQGDRYG----KASGLTFF 641
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1934323370 543 IVKDIVERMGGTIELESEENVGSTFTVTVPFEID 576
Cdd:PRK10618  642 LCNQLCRKLGGHLTIKSREGLGTRYSIHLKMLAA 675
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
599-722 3.00e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 51.85  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEatkAIRMLeREDAKKIP 678
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTG---DYDLIILDIMLPDVNGWD---IVRML-RSANKGMP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLTK 722
Cdd:PRK09836   75 ILLLTALGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRR 118
PLN03029 PLN03029
type-a response regulator protein; Provisional
600-722 3.53e-07

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 51.57  E-value: 3.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIF-----------------QNSRLDEYDVIIMDVMMPVMDGLEA 662
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLglheddrsnpdtpsvspNSHQEVEVNLIITDYCMPGMTGYDL 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 663 TKAIRmlEREDAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKPI---DIPRLKRAITKLLTK 722
Cdd:PLN03029   91 LKKIK--ESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVqlsDLNRLKPHMMKTKSK 151
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
599-671 4.26e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 52.58  E-value: 4.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934323370 599 RVLLVEDnvinMEIAHAIL------EEEHLNITEAKNGKEAFEifqNSRLDEYDVIIMDVMMPVMDGLEATKAIrMLER 671
Cdd:PRK12555    2 RIGIVND----SPLAVEALrralarDPDHEVVWVATDGAQAVE---RCAAQPPDVILMDLEMPRMDGVEATRRI-MAER 72
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
600-708 5.67e-07

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: 48.56  E-value: 5.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMPVMDGLEATKAIRMleredAK-KIP 678
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDL---GKLYDYDIILLDLNLPDMSGYEVLRTLRL-----AKvKTP 72
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPID 708
Cdd:cd17616    73 ILILSGLADIEDKVKGLGFGADDYMTKPFH 102
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 6.53e-07

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: 48.30  E-value: 6.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNA------IKYNHFHGTVNVhceELSDDGNIAVfqfVCSDTGLGMSEEFQKHAFDAFAqegkqsTTTFSG 536
Cdd:cd16944     5 ISQVLTNILKNAaeaiegRPSDVGEVRIRV---EADQDGRIVL---IVCDNGKGFPREMRHRATEPYV------TTRPKG 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 537 SGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16944    73 TGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
635-711 1.00e-06

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 50.45  E-value: 1.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1934323370 635 EIFQNSRLDEYDVIIMDVMMPVMDGLEATKAIRMLEredakKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:PRK10710   45 EVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRRFS-----DIPIVMVTAKIEEIDRLLGLEIGADDYICKPYS-PR 115
pleD PRK09581
response regulator PleD; Reviewed
594-708 1.00e-06

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 51.83  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 594 DLSGKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldeYDVIIMDVMMPVMDGLEATKAIRMLERed 673
Cdd:PRK09581  152 KDEDGRILLVDDDVSQAERIANILKEEFRVVVVSDPSEALFNAAETN----YDLVIVSANFENYDPLRLCSQLRSKER-- 225
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 674 AKKIPIIAMtANAFEEDR--KAcLEAGMNEHIGKPID 708
Cdd:PRK09581  226 TRYVPILLL-VDEDDDPRlvKA-LELGVNDYLMRPID 260
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
466-570 1.69e-06

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: 48.01  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 466 VLMNLSSNAIKYNHFHGTVNVHceELSDDGNIAVfqfvcSDTGLGMSEEfqkhAFDAFAQEGKQSTTTFSGSGLGLSIVK 545
Cdd:cd16954    41 LLGNLLDNACKWCLEFVEVTAR--QTDGGLHLIV-----DDDGPGVPES----QRSKIFQRGQRLDEQRPGQGLGLAIAK 109
                          90       100
                  ....*....|....*....|....*
gi 1934323370 546 DIVERMGGTIELESEENVGSTFTVT 570
Cdd:cd16954   110 EIVEQYGGELSLSDSPLGGARFEVV 134
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
600-706 1.81e-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: 47.01  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFqNSRLDEYDVIIMDVMMPVMDGLEATKAIrmLEREDAKKIPI 679
Cdd:cd17582     1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVL-EDEQNEIDLILTEVDLPVSSGFKLLSYI--MRHKICKNIPV 77
                          90       100
                  ....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17582    78 IMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
599-722 2.15e-06

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 47.44  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEE-EHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLEReDAKKI 677
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDlGPGNVDEADDGREALVILLCNAPD---IIICDLKMPDMDGIEFLRHLAESHS-NAAVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMN--EHIGKPIDIPRLkraiTKLLTK 722
Cdd:cd17530    78 LMSGLDGGILESAETLAGANGLNllGTLSKPFSPEEL----TELLTK 120
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
599-706 2.34e-06

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 46.83  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNV--INMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIRMLEREdaKK 676
Cdd:cd17561     3 KVLIADDNRefVQLLEEYLNSQPDMEVVGVAHNGQEALELIEE---KEPDVLLLDIIMPHLDGIGVLEKLRRMRLE--KR 77
                          90       100       110
                  ....*....|....*....|....*....|
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17561    78 PKIIMLTAFGQEDITQRAVELGASYYILKP 107
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
600-724 2.62e-06

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: 46.76  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLN--ITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIeiVGEAENGEEALEAIEELK---PDVVFLDIQMPGLDGLELAKKL----SKLAKPP 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1934323370 678 PIIAMTA------NAFEEDRKacleagmnEHIGKPIDIPRLKRAITKLLTKKG 724
Cdd:cd17532    74 LIVFVTAydeyavEAFELNAV--------DYLLKPFSEERLAEALAKLRKRLS 118
PRK10766 PRK10766
two-component system response regulator TorR;
597-712 4.38e-06

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 48.50  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 597 GKRVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRmlEREDakk 676
Cdd:PRK10766    2 SYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVD---LILLDINLPGEDGLMLTRELR--SRST--- 73
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:PRK10766   74 VGIILVTGRTDSIDRIVGLEMGADDYVTKPLELREL 109
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
36-175 5.22e-06

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


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.99  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370   36 LSEIIHSLLQAIGNYTGADRVYVFDWETDQKDSLSnTFEWCADGVAPEIdnlQAIPVSSMP-NWVkrFENKEVIVIHDLE 114
Cdd:smart00065   2 LEELLQTILEELRQLLGADRVLIYLVDENDRGELV-LVAADGLTLPTLG---IRFPLDEGLaGRV--AETGRPLNIPDVE 75
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1934323370  115 AtknsEPEEYELLKTQEIC--SLIAVPIYANHQMNGFIGVDNPDLRQ--NEISITLLSDVGGHLG 175
Cdd:smart00065  76 A----DPLFAEDLLGRYQGvrSFLAVPLVADGELVGVLALHNKKSPRpfTEEDEELLQALANQLA 136
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
600-712 5.95e-06

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 47.88  E-value: 5.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAkngkeafEIFQNSRLD----EYDVIIMDVMMPVMDGLEAtkaIRMLEREDAk 675
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEA-------ETLQRGLLEaatrKPDLIILDLGLPDGDGIEF---IRDLRQWSA- 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1934323370 676 kIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:PRK10529   73 -IPVIVLSARSEESDKIAALDAGADDYLSKPFGIGEL 108
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
600-684 6.30e-06

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 45.94  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIPI 679
Cdd:cd17549     1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSP---DFPGVVISDIRMPGMDGLELLAQI----RELDPDLPV 73

                  ....*
gi 1934323370 680 IAMTA 684
Cdd:cd17549    74 ILITG 78
PRK15115 PRK15115
response regulator GlrR; Provisional
599-720 1.65e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 47.91  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLEredaKKIP 678
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVD---LVISDLRMDEMDGMQLFAEIQKVQ----PGMP 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK15115   80 VIILTAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDAL 121
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
599-711 1.99e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 46.49  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVinmEIAHAI---LEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIRMLEREdak 675
Cdd:PRK11083    5 TILLVEDEQ---AIADTLvyaLQSEGFTVEWFERGLPALDKLRQQP---PDLVILDVGLPDISGFELCRQLLAFHPA--- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1934323370 676 kIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDiPR 711
Cdd:PRK11083   76 -LPVIFLTARSDEVDRLVGLEIGADDYVAKPFS-PR 109
PRK10816 PRK10816
two-component system response regulator PhoP;
599-709 2.45e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 46.27  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEAtkaIRMLeREDAKKIP 678
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEH---LPDIAIVDLGLPDEDGLSL---IRRW-RSNDVSLP 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDI 709
Cdd:PRK10816   75 ILVLTARESWQDKVEVLSAGADDYVTKPFHI 105
PRK10336 PRK10336
two-component system response regulator QseB;
599-706 3.81e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 45.66  E-value: 3.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNI---TEAKNGKEAFeifqnsRLDEYDVIIMDVMMPVMDGLEATKAIrmleREDAK 675
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVdwfTQGRQGKEAL------YSAPYDAVILDLTLPGMDGRDILREW----REKGQ 71
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934323370 676 KIPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:PRK10336   72 REPVLILTARDALAERVEGLRLGADDYLCKP 102
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
460-568 4.60e-05

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 43.22  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 460 PVHLSRVLMNLSSNAIKYNHFHGTVNVHCEelSDDGNIAVFQFvcsDTGLGMSEEFQKHAFDAF-----AQEGKQSTttf 534
Cdd:cd16945     2 PFLLRQAINNLLDNAIDFSPEGGLIALQLE--ADTEGIELLVF---DEGSGIPDYALNRVFERFyslprPHSGQKST--- 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 535 sgsGLGLSIVKDIVERMGGTIELES-EENVGSTFT 568
Cdd:cd16945    74 ---GLGLAFVQEVAQLHGGRITLRNrPDGVLAFLT 105
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 4.98e-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: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKYN-HFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQEGKQSTTTFSGSGLGL 541
Cdd:cd16953     1 LGQVLRNLIGNAISFSpPDTGRITVSAMPTGKMVTISV-----EDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1934323370 542 SIVKDIVERMGGTIELESEEN----VGSTFTVTVP 572
Cdd:cd16953    76 SISRQIIEAHGGISVAENHNQpgqvIGARFTVQLP 110
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
600-706 6.39e-05

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: 42.43  E-value: 6.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFqNSRLDeyDVIIMDVMMPVMDGLEATKAIRmlEREDakkIPI 679
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGL-NARPP--DLAILDIKMPRMDGMELLQRLR--QKST---LPV 72
                          90       100
                  ....*....|....*....|....*..
gi 1934323370 680 IAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd19936    73 IFLTSKDDEIDEVFGLRMGADDYITKP 99
PRK10693 PRK10693
two-component system response regulator RssB;
625-716 6.45e-05

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 45.37  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 625 TEAKNGKEAFEIfqnsrLDEY--DVIIMDVMMPVMDGLEATKAIRMlereDAKKIPIIAMTANAFEEDRKACLEAGMNEH 702
Cdd:PRK10693    1 VLAANGVDALEL-----LGGFtpDLIICDLAMPRMNGIEFVEHLRN----RGDQTPVLVISATENMADIAKALRLGVQDV 71
                          90
                  ....*....|....*
gi 1934323370 703 IGKPI-DIPRLKRAI 716
Cdd:PRK10693   72 LLKPVkDLNRLREMV 86
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
599-698 7.16e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 44.63  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVED-----NVINMEIAhaiLEEEHLNITEAKNGKEAFEIFQnsRLDEyDVIIMDVMMPVMDGLEATKAIRMlERED 673
Cdd:PRK10651    8 TILLIDDhpmlrTGVKQLIS---MAPDITVVGEASNGEQGIELAE--SLDP-DLILLDLNMPGMNGLETLDKLRE-KSLS 80
                          90       100
                  ....*....|....*....|....*
gi 1934323370 674 AKkipIIAMTANAFEEDRKACLEAG 698
Cdd:PRK10651   81 GR---IVVFSVSNHEEDVVTALKRG 102
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
506-572 7.41e-05

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: 42.39  E-value: 7.41e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1934323370 506 DTGLGMSEEFQKHAFDAFAqegkqsTTTFSGSGLGLSIVKDIVERMGGTIELESEEnvGST-FTVTVP 572
Cdd:cd16918    50 DNGPGIPPDLQDTIFYPMV------SGRENGTGLGLAIAQNIVSQHGGVIECDSQP--GHTvFSVSLP 109
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
617-667 7.77e-05

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: 42.64  E-value: 7.77e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 617 LEEEHLNITEAKNGKEAFEIFQNSRldeYDVIIMDVMMPVMDGLEATKAIR 667
Cdd:cd19930    20 LEDDLEVVAQASNGQEALRLVLKHS---PDVAILDIEMPGRTGLEVAAELR 67
PRK09483 PRK09483
response regulator; Provisional
600-687 8.63e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 44.33  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEH-LNIT-EAKNGKEAFeifQNSRLDEYDVIIMDVMMPVMDGLEATKAIrMLEREDAKKI 677
Cdd:PRK09483    4 VLLVDDHELVRAGIRRILEDIKgIKVVgEACCGEDAV---KWCRTNAVDVVLMDMNMPGIGGLEATRKI-LRYTPDVKII 79
                          90
                  ....*....|
gi 1934323370 678 PIIAMTANAF 687
Cdd:PRK09483   80 MLTVHTENPL 89
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
600-708 2.16e-04

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 41.53  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVINMEIAHAILEEEHlNITEAKNGKEAFeiFQNSRlDEYDVIIMDVMMPVMDGLEATKAIRMLERedAKKIPI 679
Cdd:cd17539     1 VLLVDDRPSSAERIAAMLSSEH-EVVVEADPDEAL--FRAAE-GPFDLVIVSLALEDFDGLRLCSQLRSLER--TRQLPI 74
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934323370 680 IAMtANAFEEDR--KAcLEAGMNEHIGKPID 708
Cdd:cd17539    75 LAV-ADPGDRGRliRA-LEIGVNDYLVRPID 103
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
463-572 4.20e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 39.84  E-value: 4.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 463 LSRVLMNLSSNAIKynHFHG-TVNVHCEELSDDGNIAVfqfvcSDTGLGmseefqkhaFDAFAQEGkqstttfsGSGLGL 541
Cdd:cd16917     1 LYRIVQEALTNALK--HAGAsRVRVTLSYTADELTLTV-----VDDGVG---------FDGPAPPG--------GGGFGL 56
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1934323370 542 SIVKDIVERMGGTIELESEENVGSTFTVTVP 572
Cdd:cd16917    57 LGMRERAELLGGTLTIGSRPGGGTRVTARLP 87
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
600-712 6.15e-04

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: 40.11  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNV-INMEIAHAiLEEEHLNITEAKNGKEAfEIFQNSRldEYDVIIMDVMMPVMDGLEATKAIRmlerEDAKKIP 678
Cdd:cd17573     1 ILLIEDDStLGKEISKG-LNEKGYQADVAESLKDG-EYYIDIR--NYDLVLVSDKLPDGNGLSIVSRIK----EKHPSIV 72
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRL 712
Cdd:cd17573    73 VIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
473-574 8.09e-04

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.70  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 473 NAIKynhfHGTvnvhcEELSDDGNIAV--------FQFVCSDTGLGMSEEFQKHAFDAFAQEGKqstttfsGSGLGLSIV 544
Cdd:COG2972   347 NAIE----HGI-----EPKEGGGTIRIsirkegdrLVITVEDNGVGMPEEKLEKLLEELSSKGE-------GRGIGLRNV 410
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 545 KDIVERM---GGTIELESEENVGSTFTVTVPFE 574
Cdd:COG2972   411 RERLKLYygeEYGLEIESEPGEGTTVTIRIPLE 443
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
599-718 1.03e-03

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


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 39.54  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEeeHLN----ITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIrmleREDA 674
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVE--QVPgftvIGTAGTGEEALKLLKERQPD---LILLDIYLPDGNGLDLLREL----RAAG 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 675 KKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITK 718
Cdd:cd19925    73 HDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
647-718 1.18e-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: 39.11  E-value: 1.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1934323370 647 VIIMDVMMPVMDGLEATKaiRMLEREDakKIPIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITK 718
Cdd:cd17537    47 CLVLDVRMPGMSGLELQD--ELLARGS--NIPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
PRK10643 PRK10643
two-component system response regulator PmrA;
599-720 1.28e-03

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 40.79  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKIP 678
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESG---HYSLVVLDLGLPDEDGLHLLRRW----RQKKYTLP 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1934323370 679 IIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLL 720
Cdd:PRK10643   75 VLILTARDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
447-558 1.37e-03

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 41.84  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 447 EASTIRHRYLI-GSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEElsDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFAQ 525
Cdd:PRK09470  337 TVSAPPGPWPInGNPNALASALENIVRNALRYSHTKIEVAFSVDK--DGLTITV-----DDDGPGVPEEEREQIFRPFYR 409
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 526 EGKQSTTTFSGSGLGLSIVKDIVERMGGTIELE 558
Cdd:PRK09470  410 VDEARDRESGGTGLGLAIVENAIQQHRGWVKAE 442
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
632-716 1.56e-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: 40.47  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 632 EAFeiFQNSRLDEYDVIIMDVMMPVMDGLEATKaiRMLEREDAkkIPIIAMTANAfeeDRKACLEA---GMNEHIGKPID 708
Cdd:COG4566    33 EAF--LAALDPDRPGCLLLDVRMPGMSGLELQE--ELAARGSP--LPVIFLTGHG---DVPMAVRAmkaGAVDFLEKPFD 103

                  ....*...
gi 1934323370 709 IPRLKRAI 716
Cdd:COG4566   104 DQALLDAV 111
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
531-574 2.14e-03

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 40.37  E-value: 2.14e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 531 TTTFSGSGLGLSIVKDIVERMGGTIELESEENVGSTFTVTVPFE 574
Cdd:COG4585   207 PEAAPGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLA 250
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
599-706 3.51e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 38.12  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINMEIAHAILEEeHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMLEREDAKkip 678
Cdd:cd17596     2 TILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQ---VILCDQRMPGTTGVEFLKEVRERWPEVVR--- 74
                          90       100
                  ....*....|....*....|....*....
gi 1934323370 679 iIAMTANAFEEDRKACL-EAGMNEHIGKP 706
Cdd:cd17596    75 -IIISGYTDSEDIIAGInEAGIYQYLTKP 102
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
491-572 4.21e-03

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 40.20  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 491 LSDDGNIAVFQfvCSDTGLGMSEEFQKHAFdafaQEGKQSTTTFSGS-GLGLSIVKDIVERMGGTIELESEENVGSTFTV 569
Cdd:PRK15053  462 LSDEGDDVVIE--VADQGCGVPESLRDKIF----EQGVSTRADEPGEhGIGLYLIASYVTRCGGVITLEDNDPCGTLFSI 535

                  ...
gi 1934323370 570 TVP 572
Cdd:PRK15053  536 FIP 538
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
646-706 4.26e-03

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: 37.35  E-value: 4.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1934323370 646 DVIIMDVMMPVMDGLEATKAIRMLERedAKKIPIIAMTANAFEEDRKACLEAGMNEHIGKP 706
Cdd:cd17602    44 DLILIDIDMPDLDGYELCSLLRKSSA--LKDTPIIMLTGKDGLVDRIRAKMAGASGYLTKP 102
PRK13435 PRK13435
response regulator; Provisional
593-719 5.12e-03

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 38.11  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 593 MDLSGKRVLLVED-NVINMEIAHAILEEEHLNITEAKNGKEAFEIfqnSRLDEYDVIIMDVMMpvMDGLEATKAIRMLER 671
Cdd:PRK13435    1 MFLRQLKVLIVEDeALIALELEKLVEEAGHEVVGIAMSSEQAIAL---GRRRQPDVALVDVHL--ADGPTGVEVARRLSA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1934323370 672 EdaKKIPIIAMTANAfeeDRKACLEAGMNEHIGKPIDIPRLKRAITKL 719
Cdd:PRK13435   76 D--GGVEVVFMTGNP---ERVPHDFAGALGVIAKPYSPRGVARALSYL 118
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
599-705 6.61e-03

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 37.39  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 599 RVLLVEDNVINME-IAHAILEEEHLNITEAKNGKEAFEIFQNSRLDeydVIIMDVMMPVMDGLEATKAIRMleREDAKKI 677
Cdd:cd17575     2 MVLLVDDQAIIGEaVRRALADEEDIDFHYCSDPTEAIEVASQIKPT---VILQDLVMPGVDGLTLVRFFRA--NPATRDI 76
                          90       100
                  ....*....|....*....|....*...
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGK 705
Cdd:cd17575    77 PIIVLSTKEEPEVKSEAFALGANDYLVK 104
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
600-709 7.05e-03

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: 36.88  E-value: 7.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDNVInmeIAHAI---LEEEHLNITEAKNGKEAFEIFQNSrldEYDVIIMDVMMPVMDGLEATKAIRMLeredaKK 676
Cdd:cd18159     1 ILIVEDDET---IASLLkkhLEKWGYEVVLIEDFEDVLEEFLQF---KPDLVLLDINLPYFDGFYWCREIRQI-----SN 69
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1934323370 677 IPIIAMTANAFEEDRKACLEAGMNEHIGKPIDI 709
Cdd:cd18159    70 VPIIFISSRDDNMDQVMAINMGGDDYITKPFDL 102
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
644-706 8.01e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 36.33  E-value: 8.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1934323370 644 EYDVIIMDVMMPVMDGLEATKAIRMlEREDakkIPIIAMTA-NAFEEDRKAClEAGMNEHIGKP 706
Cdd:cd19928    42 EGDLVITDVVMPDENGLDLIPRIKK-ARPD---LPIIVMSAqNTLMTAVKAA-ERGAFEYLPKP 100
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
458-558 8.44e-03

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 39.18  E-value: 8.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 458 GSPVHLSRVLMNLSSNAIKYNHFHGTVNVHCEELSDDGNIAVfqfvcSDTGLGMSEEFQKHAFDAFaqegKQSTTTFSGS 537
Cdd:PRK10755  243 GDATLLRLLLRNLVENAHRYSPEGSTITIKLSQEDGGAVLAV-----EDEGPGIDESKCGELSKAF----VRMDSRYGGI 313
                          90       100
                  ....*....|....*....|.
gi 1934323370 538 GLGLSIVKDIVERMGGTIELE 558
Cdd:PRK10755  314 GLGLSIVSRITQLHHGQFFLQ 334
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
646-717 8.59e-03

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 39.08  E-value: 8.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1934323370 646 DVIIMDVMMPVMDGLEATKAIrmleREDAKKIPIIAMTANAfeeDRKACLEA---GMNEHIGKPIDIPR----LKRAIT 717
Cdd:PRK10923   49 DVLLSDIRMPGMDGLALLKQI----KQRHPMLPVIIMTAHS---DLDAAVSAyqqGAFDYLPKPFDIDEavalVERAIS 120
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
600-721 9.07e-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: 36.56  E-value: 9.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1934323370 600 VLLVEDN-VINMEIAHAILEEEHLN-ITEAKNGKEAFEIFQNsrlDEYDVIIMDVMMPVMDGLEATKAIrmleREDAKKI 677
Cdd:cd19931     1 VLLIDDHpLLRKGIKQLIELDPDFTvVGEASSGEEGIELAER---LDPDLILLDLNMKGMSGLDTLKAL----REEGVSA 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1934323370 678 PIIAMTANAFEEDRKACLEAGMNEHIGKPIDIPRLKRAITKLLT 721
Cdd:cd19931    74 RIVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
 
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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