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Conserved domains on  [gi|2047656081|dbj|BBL75270|]
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hypothetical protein MishRS11D_23680 [Methylomagnum ishizawai]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
420-1032 1.37e-133

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


:

Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 418.82  E-value: 1.37e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  420 PQLLDILLQELPLHTRQFAESAQRLGAGGGLHD-LETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSACSKEGRMPGP 498
Cdd:COG0643      4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  499 ALARTLLDAADCLEAMGEALQGRGTPPAEARTVLQEVLDWANRIDRDGLSALDAPDAPAPAHPADTQDGAPAPPAPQDTP 578
Cdd:COG0643     84 ELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAAAPPAEAAAAAAE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  579 G----TSTVRVPTAWIESLLRLSGESLVHSAQaherlrrikiqlqamraqfesLQGLGAELEElidvrdwsgpaggtggq 654
Cdd:COG0643    164 AaaaaSETVRVDVERLDRLMNLVGELVITRAR---------------------LEQLAEELED----------------- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  655 dfdnlemdqynelhtasrrlveaavdareigldigKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQ 734
Cdd:COG0643    206 -----------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRD 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  735 TCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDG 814
Cdd:COG0643    251 LARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDG 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  815 RGLDLGAIHATAVKRGLLEPGQAA--TPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGL 892
Cdd:COG0643    331 RGLDLEKIRAKAIEKGLITAEEAAalSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGT 410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  893 GVELRIPLPLSRSLALLAQVGPHRVAIVNKGLEQIRH--RDDAEPGGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRG 970
Cdd:COG0643    411 TFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRldPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERG 490
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  971 VLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVIDLPELLR 1032
Cdd:COG0643    491 PVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1062-1177 2.24e-38

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


:

Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 139.60  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:COG0784      9 LVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALTAY 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG0784     89 ADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
420-1032 1.37e-133

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 418.82  E-value: 1.37e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  420 PQLLDILLQELPLHTRQFAESAQRLGAGGGLHD-LETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSACSKEGRMPGP 498
Cdd:COG0643      4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  499 ALARTLLDAADCLEAMGEALQGRGTPPAEARTVLQEVLDWANRIDRDGLSALDAPDAPAPAHPADTQDGAPAPPAPQDTP 578
Cdd:COG0643     84 ELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAAAPPAEAAAAAAE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  579 G----TSTVRVPTAWIESLLRLSGESLVHSAQaherlrrikiqlqamraqfesLQGLGAELEElidvrdwsgpaggtggq 654
Cdd:COG0643    164 AaaaaSETVRVDVERLDRLMNLVGELVITRAR---------------------LEQLAEELED----------------- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  655 dfdnlemdqynelhtasrrlveaavdareigldigKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQ 734
Cdd:COG0643    206 -----------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRD 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  735 TCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDG 814
Cdd:COG0643    251 LARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDG 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  815 RGLDLGAIHATAVKRGLLEPGQAA--TPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGL 892
Cdd:COG0643    331 RGLDLEKIRAKAIEKGLITAEEAAalSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGT 410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  893 GVELRIPLPLSRSLALLAQVGPHRVAIVNKGLEQIRH--RDDAEPGGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRG 970
Cdd:COG0643    411 TFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRldPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERG 490
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  971 VLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVIDLPELLR 1032
Cdd:COG0643    491 PVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552
CheA_Halo NF041336
chemotaxis protein CheA;
662-1026 7.71e-60

chemotaxis protein CheA;


Pssm-ID: 469233 [Multi-domain]  Cd Length: 666  Bit Score: 218.37  E-value: 7.71e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  662 DQYNELHTASRRLVEAAVDAREIGLDigKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGK 741
Cdd:NF041336   299 DQLDQLYGLVEQLVTSRIKLRRAVEE--EDLVSAEDELEELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGK 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  742 QAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGA 821
Cdd:NF041336   377 EIDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEE 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  822 IHATAVKRGLL--EPGQAATPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIP 899
Cdd:NF041336   457 IREKAIEKGVKteEELEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLP 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  900 LPLSRSLALLAQVGPHRVAIVNKGLEQIRHRDDAEP-GGDPAwARLDGLDYPAATLRGLLRVP-RRPDGDgrGVLLLARA 977
Cdd:NF041336   537 VTVAIVKVLFVTVGDEEYGIPIKNVDEISRLEDVETvNGREV-ITHDDEIYPLVSLGDALDVPgETRNGD--GMLVRIRE 613
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2047656081  978 ADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVID 1026
Cdd:NF041336   614 SERQVALHCDDVVGQEEVVVKPFEGILSGTPGLSGTAVLGDGEVVHILD 662
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
724-899 1.26e-55

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: 190.87  E-value: 1.26e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  724 LLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREG 803
Cdd:cd16916      1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  804 GQVRVHCQDDGRGLDLGAIHATAVKRGLLEPGQAA--TPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGS 881
Cdd:cd16916     81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAAtlSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160
                          170
                   ....*....|....*...
gi 2047656081  882 LALDSTPGAGLGVELRIP 899
Cdd:cd16916    161 IEVESEPGQGTTFTIRLP 178
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
693-1030 6.54e-44

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 170.68  E-value: 6.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  693 DALNeTLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRN 772
Cdd:PRK10547   318 DLIT-SMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  773 AVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGAIHATAVKRGlLEPGQAATPRELSELILRPNF 852
Cdd:PRK10547   397 SLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQG-LAVSENMSDEEVGMLIFAPGF 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  853 STRERATQTSGRGVGMDAVRARVIALGGSLALDSTpgAGLGVELRIPLPLsrSLALL----AQVGpHRVAI--VNKGLEQ 926
Cdd:PRK10547   476 STAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSK--QGKGTTIRILLPL--TLAILdgmsVRVA-DEVFIlpLNAVMES 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  927 IRHR-DDAEP-GGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGPYL 1004
Cdd:PRK10547   551 LQPReEDLHPlAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 630
                          330       340
                   ....*....|....*....|....*.
gi 2047656081 1005 AKPPGVIGATVLGDGAVVPVIDLPEL 1030
Cdd:PRK10547   631 RKVPGISAATILGDGSVALIVDVSAL 656
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1062-1177 2.24e-38

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 139.60  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:COG0784      9 LVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALTAY 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG0784     89 ADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1062-1172 1.80e-33

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: 124.89  E-value: 1.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYG-RLPIVMITS 1140
Cdd:cd17546      2 LVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGrRTPIIALTA 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd17546     82 NALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1062-1173 5.36e-27

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: 106.47  E-value: 5.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeyGRLPIVMITSR 1141
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
pleD PRK09581
response regulator PleD; Reviewed
1062-1176 6.06e-20

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 94.58  E-value: 6.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMIT-- 1139
Cdd:PRK09581     6 LVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTal 85
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2047656081 1140 SRTTQRHRKLaaEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK09581    86 DDPEDRVRGL--EAGADDFLTKPINDVALFARVKSLT 120
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
761-901 1.24e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 82.31  E-value: 1.24e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081   761 ALADPLMHLLRNAVDHGLESPeeravlgkPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatP 840
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYT--------PEGGRITVTLERDGDHVEITVEDNGPGI----------------------P 50
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047656081   841 RELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLP 901
Cdd:smart00387   51 PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1062-1113 4.61e-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: 61.82  E-value: 4.61e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMP 1113
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
763-901 5.46e-11

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: 60.46  E-value: 5.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  763 ADPLMHLLRNAVDHGLESpeeravlgKPQAGRIVIAFEReGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRE 842
Cdd:pfam02518    3 ELRLRQVLSNLLDNALKH--------AAKAGEITVTLSE-GGELTLTVEDNGIGI----------------------PPE 51
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2047656081  843 LSELILRPnFSTRERaTQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLP 901
Cdd:pfam02518   52 DLPRIFEP-FSTADK-RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
 
Name Accession Description Interval E-value
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
420-1032 1.37e-133

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 418.82  E-value: 1.37e-133
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  420 PQLLDILLQELPLHTRQFAESAQRLGAGGGLHD-LETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSACSKEGRMPGP 498
Cdd:COG0643      4 DELLEIFLEEARELLEQLEEGLLALEQDPDDPElLNAIFRAAHTLKGSAGMLGLDALAELAHALEDLLDALRNGELALTP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  499 ALARTLLDAADCLEAMGEALQGRGTPPAEARTVLQEVLDWANRIDRDGLSALDAPDAPAPAHPADTQDGAPAPPAPQDTP 578
Cdd:COG0643     84 ELIDLLLEALDALRALLDALEAGGEPPADISALLARLDASEEAIEEVVADEVEISPPAPAALEPAPAAAPPAEAAAAAAE 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  579 G----TSTVRVPTAWIESLLRLSGESLVHSAQaherlrrikiqlqamraqfesLQGLGAELEElidvrdwsgpaggtggq 654
Cdd:COG0643    164 AaaaaSETVRVDVERLDRLMNLVGELVITRAR---------------------LEQLAEELED----------------- 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  655 dfdnlemdqynelhtasrrlveaavdareigldigKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQ 734
Cdd:COG0643    206 -----------------------------------ESLRELEEALEQLSRLTRELQDGVMRLRMVPISTVFNRFPRMVRD 250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  735 TCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDG 814
Cdd:COG0643    251 LARELGKEVELVIEGEETELDRTVLERLGDPLVHLVRNAVDHGIETPEERLAAGKPETGTITLSAYHEGGRVVIEVSDDG 330
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  815 RGLDLGAIHATAVKRGLLEPGQAA--TPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGL 892
Cdd:COG0643    331 RGLDLEKIRAKAIEKGLITAEEAAalSDEELLELIFAPGFSTAEEVTDLSGRGVGMDVVKTNIEALGGTIEIESEPGKGT 410
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  893 GVELRIPLPLSRSLALLAQVGPHRVAIVNKGLEQIRH--RDDAEPGGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRG 970
Cdd:COG0643    411 TFTLRLPLTLAIIDGLLVRVGGETYAIPLSSVEEVLRldPDDIETVEGREVIRLRGELLPLVRLGELLGLPGAEPEGERG 490
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  971 VLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVIDLPELLR 1032
Cdd:COG0643    491 PVVVVRSGGRRVALVVDELLGQQEVVIKPLGPLLRRVPGISGATILGDGRVALILDVAALVR 552
CheA_Halo NF041336
chemotaxis protein CheA;
662-1026 7.71e-60

chemotaxis protein CheA;


Pssm-ID: 469233 [Multi-domain]  Cd Length: 666  Bit Score: 218.37  E-value: 7.71e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  662 DQYNELHTASRRLVEAAVDAREIGLDigKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGK 741
Cdd:NF041336   299 DQLDQLYGLVEQLVTSRIKLRRAVEE--EDLVSAEDELEELGKITASLQDTVMDMRLVPLKKIVGKFPRLVRDLARDQGK 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  742 QAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGA 821
Cdd:NF041336   377 EIDFTIEGEDIELDRTILTELSDPLMHLLRNAVDHGIEPPEEREAKGKPREGTIELRAERERDHVSITVEDDGAGLDVEE 456
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  822 IHATAVKRGLL--EPGQAATPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIP 899
Cdd:NF041336   457 IREKAIEKGVKteEELEAMDDSEVYDLVFHPGFSTTEEVTDVSGRGVGMDVVHQTVRGLDGSVNVESEPGEGTTVTLRLP 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  900 LPLSRSLALLAQVGPHRVAIVNKGLEQIRHRDDAEP-GGDPAwARLDGLDYPAATLRGLLRVP-RRPDGDgrGVLLLARA 977
Cdd:NF041336   537 VTVAIVKVLFVTVGDEEYGIPIKNVDEISRLEDVETvNGREV-ITHDDEIYPLVSLGDALDVPgETRNGD--GMLVRIRE 613
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 2047656081  978 ADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVID 1026
Cdd:NF041336   614 SERQVALHCDDVVGQEEVVVKPFEGILSGTPGLSGTAVLGDGEVVHILD 662
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
724-899 1.26e-55

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: 190.87  E-value: 1.26e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  724 LLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGLESPEERAVLGKPQAGRIVIAFEREG 803
Cdd:cd16916      1 VFSRFPRLVRDLARELGKQVELVVEGEDTELDKSVLEKLADPLTHLLRNAVDHGIEAPEERLAAGKPPEGTITLRAEHQG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  804 GQVRVHCQDDGRGLDLGAIHATAVKRGLLEPGQAA--TPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGS 881
Cdd:cd16916     81 NQVVIEVSDDGRGIDREKIREKAIERGLITADEAAtlSDDEVLNLIFAPGFSTAEQVTDVSGRGVGMDVVKRSIESLGGT 160
                          170
                   ....*....|....*...
gi 2047656081  882 LALDSTPGAGLGVELRIP 899
Cdd:cd16916    161 IEVESEPGQGTTFTIRLP 178
PRK10547 PRK10547
chemotaxis protein CheA; Provisional
693-1030 6.54e-44

chemotaxis protein CheA; Provisional


Pssm-ID: 236712 [Multi-domain]  Cd Length: 670  Bit Score: 170.68  E-value: 6.54e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  693 DALNeTLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRN 772
Cdd:PRK10547   318 DLIT-SMGQLQRNARDLQESVMSIRMMPMEYVFSRFPRLVRDLAGKLGKQVELTLVGSSTELDKSLIERIIDPLTHLVRN 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  773 AVDHGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGAIHATAVKRGlLEPGQAATPRELSELILRPNF 852
Cdd:PRK10547   397 SLDHGIELPEKRLAAGKNSVGNLILSAEHQGGNICIEVTDDGAGLNRERILAKAASQG-LAVSENMSDEEVGMLIFAPGF 475
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  853 STRERATQTSGRGVGMDAVRARVIALGGSLALDSTpgAGLGVELRIPLPLsrSLALL----AQVGpHRVAI--VNKGLEQ 926
Cdd:PRK10547   476 STAEQVTDVSGRGVGMDVVKRNIQEMGGHVEIQSK--QGKGTTIRILLPL--TLAILdgmsVRVA-DEVFIlpLNAVMES 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  927 IRHR-DDAEP-GGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGPYL 1004
Cdd:PRK10547   551 LQPReEDLHPlAGGERVLEVRGEYLPLVELWKVFDVAGAKTEATQGIVVILQSAGRRYALLVDQLIGQHQVVVKNLESNY 630
                          330       340
                   ....*....|....*....|....*.
gi 2047656081 1005 AKPPGVIGATVLGDGAVVPVIDLPEL 1030
Cdd:PRK10547   631 RKVPGISAATILGDGSVALIVDVSAL 656
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1062-1177 2.24e-38

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 139.60  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:COG0784      9 LVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPIIALTAY 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG0784     89 ADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1062-1172 2.09e-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: 133.11  E-value: 2.09e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:COG3706      5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTAL 84
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:COG3706     85 DDEEDRARALEAGADDYLTKPFDPEELLARV 115
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1062-1172 1.80e-33

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: 124.89  E-value: 1.80e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYG-RLPIVMITS 1140
Cdd:cd17546      2 LVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGrRTPIIALTA 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd17546     82 NALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1059-1177 3.92e-33

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: 127.97  E-value: 3.92e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMI 1138
Cdd:COG3437      7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFL 86
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG3437     87 TALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1062-1176 2.92e-32

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: 124.68  E-value: 2.92e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeyGRLPIVMITSR 1141
Cdd:COG0745      5 LVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARP--SDIPIIMLTAR 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:COG0745     83 DDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1062-1162 1.23e-28

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: 110.78  E-value: 1.23e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPP--DIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1062-1175 9.47e-28

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: 108.68  E-value: 9.47e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGY-RVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITS 1140
Cdd:cd17551      4 LIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMITA 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGL 1175
Cdd:cd17551     84 DTDREVRLRALEAGATDFLTKPFDPVELLARVRNL 118
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1062-1172 4.99e-27

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: 106.39  E-value: 4.99e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd17580     82 GQPEDRERALEAGFDAHLVKPVDPDELIELI 112
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1062-1173 5.36e-27

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: 106.47  E-value: 5.36e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeyGRLPIVMITSR 1141
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRD--PTTPVIILTAH 79
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:pfam00072   80 GDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1062-1163 5.06e-26

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: 103.35  E-value: 5.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17538      3 LVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITAL 82
                           90       100
                   ....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPV 1163
Cdd:cd17538     83 DDREDRIRGLEAGADDFLSKPI 104
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1062-1177 2.20e-25

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: 110.44  E-value: 2.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSR 1141
Cdd:COG2204      6 LVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL--DPDLPVILLTGY 83
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG2204     84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1062-1162 4.34e-25

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: 100.62  E-value: 4.34e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGD-VGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMIT 1139
Cdd:COG4753      3 LIVDDEPLIREGLKRILEWeAGFEvVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIIILS 80
                           90       100
                   ....*....|....*....|...
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:COG4753     81 GYSDFEYAQEAIKLGADDYLLKP 103
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1062-1177 1.97e-24

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: 99.80  E-value: 1.97e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSN----RRALEQLlgDVGYRVQTARDGVEATELLGR-------VRPDIVLTDLEMPRMNGIELAGHIRARPEY 1130
Cdd:cd17557      3 LLVEDNPGDaeliQEAFKEA--GVPNELHVVRDGEEALDFLRGegeyadaPRPDLILLDLNMPRMDGFEVLREIKADPDL 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2047656081 1131 GRLPIVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:cd17557     81 RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRSLGE 127
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1061-1176 1.40e-23

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: 97.02  E-value: 1.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMIT 1139
Cdd:cd19923      3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd19923     83 AEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1062-1176 2.13e-23

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: 96.22  E-value: 2.13e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17562      4 LAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLTTE 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17562     84 SSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1062-1173 3.79e-23

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: 95.68  E-value: 3.79e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17548      3 LIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTAY 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17548     83 AMKGDREKILEAGCDGYISKPIDTREFLETVA 114
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1062-1162 1.46e-22

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 93.24  E-value: 1.46e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGS--DIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1062-1176 4.59e-22

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: 92.39  E-value: 4.59e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17598      2 LIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTTL 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17598     82 SDPRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1062-1173 1.27e-21

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: 91.68  E-value: 1.27e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYR--VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRA-RPeygrLPIVMI 1138
Cdd:cd17541      4 LIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAeRP----TPVVMV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2047656081 1139 TSRtTQRHRKLAAEA---GIDAYLTKPVRD---------DDLLDRIR 1173
Cdd:cd17541     80 SSL-TEEGAEITLEAlelGAVDFIAKPSGGisldleeiaEELIEKIK 125
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1062-1163 5.12e-21

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: 89.11  E-value: 5.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd19920      2 LIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTAL 81
                           90       100
                   ....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPV 1163
Cdd:cd19920     82 TDTEDKVKGFELGAVDYITKPF 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1062-1173 3.39e-20

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 87.18  E-value: 3.39e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLG--DVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMIT 1139
Cdd:cd17535      2 LIVDDHPLVREGLRRLLEsePDIEVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR--YPDLKVIVLT 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17535     80 AHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIR 113
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1062-1176 3.45e-20

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: 86.94  E-value: 3.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPRELLARVKAVL 115
pleD PRK09581
response regulator PleD; Reviewed
1062-1176 6.06e-20

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 94.58  E-value: 6.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMIT-- 1139
Cdd:PRK09581     6 LVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTal 85
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2047656081 1140 SRTTQRHRKLaaEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK09581    86 DDPEDRVRGL--EAGADDFLTKPINDVALFARVKSLT 120
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1062-1177 7.14e-20

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 86.95  E-value: 7.14e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDV-GYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMIT 1139
Cdd:COG4565      7 LIVEDDPMVAELLRRYLERLpGFEvVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGP--DVDVIVIT 84
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG4565     85 AARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1061-1162 8.81e-20

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: 85.89  E-value: 8.81e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRP---------DIVLTDLEMPRMNGIELAGHIRARPEYG 1131
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskelDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 2047656081 1132 RLPIVMITSRTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19924     81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
1062-1170 1.29e-19

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 95.04  E-value: 1.29e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRarpEYGR-LPIVMITS 1140
Cdd:PRK10841   805 LVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLR---QLGLtLPVIGVTA 881
                           90       100       110
                   ....*....|....*....|....*....|
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLD 1170
Cdd:PRK10841   882 NALAEEKQRCLEAGMDSCLSKPVTLDVLKQ 911
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1062-1177 1.49e-19

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: 85.47  E-value: 1.49e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLL--GDVGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMI 1138
Cdd:cd17536      2 LIVDDEPLIREGLKKLIdwEELGFEvVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL--YPDIKIIIL 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2047656081 1139 TSrttqrH------RKlAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:cd17536     80 SG-----YddfeyaQK-AIRLGVVDYLLKPVDEEELEEALEKAKE 118
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1062-1176 4.01e-19

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: 84.22  E-value: 4.01e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd17618      4 LIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLTAR 83
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17618     84 GEEEDKVRGLEAGADDYITKPFSPRELVARIKAVL 118
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1062-1175 5.70e-19

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: 83.42  E-value: 5.70e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSR 1141
Cdd:cd17554      4 LVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVIICTAY 81
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRH--RKLAAeagiDAYLTKPVRDDDLLDRIRGL 1175
Cdd:cd17554     82 SEYKSdfSSWAA----DAYVVKSSDLTELKETIKRL 113
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1062-1176 5.83e-19

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: 83.59  E-value: 5.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:cd17627      2 LVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILVLTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17627     80 DSVSDRVAGLDAGADDYLVKPFALEELLARVRALL 114
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
761-901 1.24e-18

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 82.31  E-value: 1.24e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081   761 ALADPLMHLLRNAVDHGLESPeeravlgkPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatP 840
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYT--------PEGGRITVTLERDGDHVEITVEDNGPGI----------------------P 50
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047656081   841 RELSELILRPNFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLP 901
Cdd:smart00387   51 PEDLEKIFEPFFRTDKRSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1062-1162 4.49e-18

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: 80.50  E-value: 4.49e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:cd19927      2 LLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTAK 81
                           90       100
                   ....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19927     82 GMTSDRIKGYNAGCDGYLSKP 102
orf27 CHL00148
Ycf27; Reviewed
1062-1176 4.76e-18

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 84.77  E-value: 4.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSR 1141
Cdd:CHL00148    10 LVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD---VPIIMLTAL 86
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:CHL00148    87 GDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1062-1172 6.20e-18

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: 80.92  E-value: 6.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpEYGrlPIVMITS 1140
Cdd:cd19932      4 LIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE-NIA--PIVLLTA 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd19932     81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1062-1176 6.75e-18

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: 80.54  E-value: 6.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSR 1141
Cdd:cd17614      2 LVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN---VPIIMLTAK 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17614     79 DSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1061-1169 1.11e-17

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: 82.31  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeygRLPIVMIT 1139
Cdd:COG3707      6 VLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEER---PAPVILLT 82
                           90       100       110
                   ....*....|....*....|....*....|
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLL 1169
Cdd:COG3707     83 AYSDPELIERALEAGVSAYLVKPLDPEDLL 112
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1061-1178 1.27e-17

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 83.33  E-value: 1.27e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDV-GYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMI 1138
Cdd:COG3279      4 ILIVDDEPLARERLERLLEKYpDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDP--PPPIIFT 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2047656081 1139 TSrttqrHRKLAAEA----GIDaYLTKPVRDDDL---LDRIRGLLET 1178
Cdd:COG3279     82 TA-----YDEYALEAfevnAVD-YLLKPIDEERLakaLEKAKERLEA 122
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1062-1169 1.34e-17

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: 79.76  E-value: 1.34e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQ-TARDGVEATELLGRVRPDIVLTDLEMP-RMNGIELAGHIRarpEYGRLPIVMIT 1139
Cdd:cd17534      4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR---EKFDIPVIFLT 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLL 1169
Cdd:cd17534     81 AYSDEETLERAKETNPYGYLVKPFNERELK 110
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1062-1176 1.41e-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: 79.63  E-value: 1.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMITS 1140
Cdd:cd17542      4 LIVDDAAFMRMMLKDILTKAGYEvVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK--VIMCSA 81
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17542     82 MGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1061-1162 3.01e-17

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: 79.10  E-value: 3.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRvRPDI--VLTDLEMPRMNGIELAGHIRARPEYGRLPIVMI 1138
Cdd:cd17544      3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQ-HPDIklVITDYNMPEMDGFELVREIRKKYSRDQLAIIGI 81
                           90       100
                   ....*....|....*....|....*..
gi 2047656081 1139 TSrttQRHRKLAAE---AGIDAYLTKP 1162
Cdd:cd17544     82 SA---SGDNALSARfikAGANDFLTKP 105
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1062-1177 4.09e-17

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: 78.21  E-value: 4.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRAR-PEYGRLpivMITS 1140
Cdd:cd17569      4 LLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERyPDTVRI---LLTG 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2047656081 1141 rttqrHRKLAA------EAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:cd17569     81 -----YADLDAaieainEGEIYRFLTKPWDDEELKETIRQALE 118
CheA_reg cd00731
CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. ...
943-1030 1.02e-16

CheA regulatory domain; CheA is a histidine protein kinase present in bacteria and archea. Activated by the chemotaxis receptor a histidine phosphoryl group from CheA is passed directly to an aspartate in the response regulator CheY. This signalling mechanism is modulated by the methyl accepting chemotaxis proteins (MCPs). MCPs form a highly interconnected, tightly packed array within the membrane that is organized, at least in part, through interactions with CheW and CheA. The CheA regulatory domain belongs to the family of CheW_like proteins and has been proposed to mediate interaction with the kinase regulator CheW.


Pssm-ID: 238373 [Multi-domain]  Cd Length: 132  Bit Score: 77.60  E-value: 1.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  943 RLDGLDYPAATLRGLLRVPRRPDGDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVV 1022
Cdd:cd00731     45 NVRGELLPLVRLGELFNVRGENEEPDEGVVVVVRTGGRKAALVVDQIIGQEEVVIKPLGGFLSNIPGISGATILGDGRVA 124

                   ....*...
gi 2047656081 1023 PVIDLPEL 1030
Cdd:cd00731    125 LILDVPAL 132
PRK10610 PRK10610
chemotaxis protein CheY;
1062-1177 2.61e-16

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 76.55  E-value: 2.61e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITS 1140
Cdd:PRK10610     9 LVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTA 88
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:PRK10610    89 EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1062-1139 6.37e-16

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: 74.84  E-value: 6.37e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMIT 1139
Cdd:cd17550      2 LIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEK--YPDLPVIMIS 77
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1062-1176 1.15e-15

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: 74.26  E-value: 1.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSR 1141
Cdd:cd17623      2 LLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ---VPVLMLTAR 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17623     79 GDDIDRILGLELGADDYLPKPFNPRELVARIRAIL 113
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1062-1177 3.43e-15

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: 73.29  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRAR-PEygrLPIVMITS 1140
Cdd:cd17549      2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELdPD---LPVILITG 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2047656081 1141 rttqrHR--KLAAEA---GidAY--LTKPVRDDDLLDRIRGLLE 1177
Cdd:cd17549     79 -----HGdvPMAVEAmraG--AYdfLEKPFDPERLLDVVRRALE 115
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1062-1173 4.61e-15

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: 72.42  E-value: 4.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGrlpIVMITSR 1141
Cdd:cd17619      4 LIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEVG---IILVTGR 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17619     81 DDEVDRIVGLEIGADDYVTKPFNPRELLVRAK 112
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1062-1176 5.23e-15

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 75.61  E-value: 5.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRvRPDIVLTDLEMPRMNGIELAGHIRarpEYGRLPIVMITSR 1141
Cdd:PRK10955     5 LLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD-SIDLLLLDVMMPKKNGIDTLKELR---QTHQTPVIMLTAR 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK10955    81 GSELDRVLGLELGADDYLPKPFNDRELVARIRAIL 115
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
1062-1173 8.29e-15

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 77.50  E-value: 8.29e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGD------VGyrvqTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHI-RARPeygrLP 1134
Cdd:PRK00742     7 LVVDDSAFMRRLISEILNSdpdievVG----TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKImRLRP----TP 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2047656081 1135 IVMITSRTTQrhrklAAEAGIDA-------YLTKPVRD---------DDLLDRIR 1173
Cdd:PRK00742    79 VVMVSSLTER-----GAEITLRAlelgavdFVTKPFLGislgmdeykEELAEKVR 128
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1063-1177 9.86e-15

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: 73.98  E-value: 9.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeyGRLPIVMITSR- 1141
Cdd:COG4566      4 IVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARG--SPLPVIFLTGHg 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2047656081 1142 ---TTQRhrklAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:COG4566     82 dvpMAVR----AMKAGAVDFLEKPFDDQALLDAVRRALA 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1062-1162 1.76e-14

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: 70.27  E-value: 1.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRarpEYGRLPIVMITSR 1141
Cdd:cd17620      2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLR---EWSAVPVIVLSAR 78
                           90       100
                   ....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd17620     79 DEESDKIAALDAGADDYLTKP 99
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1059-1183 2.41e-14

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 72.26  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYgrLPIVMI 1138
Cdd:COG4567      5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPD--ARIVVL 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2047656081 1139 T---SRTTqrhrklAAEA---GIDAYLTKPVRDDDLLDRIRGLLETGLALP 1183
Cdd:COG4567     83 TgyaSIAT------AVEAiklGADDYLAKPADADDLLAALERAEGDAPAPP 127
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1062-1176 4.82e-14

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: 69.42  E-value: 4.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSR 1141
Cdd:cd17626      4 LVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAESG---VPIVMLTAK 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17626     81 SDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1062-1168 9.72e-14

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: 68.81  E-value: 9.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLgRVRP---DIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMI 1138
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSML-RENKdefDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDL 1168
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1061-1176 1.89e-13

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: 68.15  E-value: 1.89e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRArpEYGRLPIVMITS 1140
Cdd:cd17615      2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRA--DGPDVPVLFLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17615     80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLRALL 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1062-1176 2.29e-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: 67.51  E-value: 2.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSR 1141
Cdd:cd17624      2 LLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQ--GQSLPVLILTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17624     80 DGVDDRVAGLDAGADDYLVKPFALEELLARLRALL 114
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1062-1176 2.48e-13

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: 67.40  E-value: 2.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRarpEYGRLPIVMITSR 1141
Cdd:cd19939      3 LIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR---EHSHVPILMLTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd19939     80 TEEMDRVLGLEMGADDYLCKPFSPRELLARVRALL 114
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1062-1177 2.82e-13

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 73.73  E-value: 2.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:PRK11361     8 LIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHET--RTPVILMTAY 85
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:PRK11361    86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1062-1176 3.10e-13

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 67.25  E-value: 3.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRArpEYGRLPIVMITSR 1141
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE--EGIETPVLLLTAL 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1060-1173 3.33e-13

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: 67.09  E-value: 3.33e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1060 LALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMIT 1139
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD---VPIIIIS 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1140 SRTTQR-HRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17594     78 GDRRDEiDRVVGLELGADDYLAKPFGLRELLARVR 112
PRK10766 PRK10766
two-component system response regulator TorR;
1062-1176 3.76e-13

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 70.07  E-value: 3.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGrlpIVMITSR 1141
Cdd:PRK10766     6 LVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTVG---IILVTGR 82
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK10766    83 TDSIDRIVGLEMGADDYVTKPLELRELLVRVKNLL 117
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1062-1176 4.08e-13

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: 66.92  E-value: 4.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeyGR-LPIVMITS 1140
Cdd:cd19934      2 LLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE---GRaTPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd19934     79 RDSWQDKVEGLDAGADDYLTKPFHIEELLARLRALI 114
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
1059-1178 4.21e-13

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: 67.39  E-value: 4.21e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLLGDvGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRAR-PEygrlPIVM 1137
Cdd:cd17596      1 PTILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERwPE----VVRI 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2047656081 1138 ITSRTTQRHRKLAA--EAGIDAYLTKPVRDDDLLDRIRGLLET 1178
Cdd:cd17596     76 IISGYTDSEDIIAGinEAGIYQYLTKPWHPDQLLLTVRNAARL 118
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1063-1173 4.30e-13

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: 66.85  E-value: 4.30e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQT---ARDGVEATELlgrVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMIT 1139
Cdd:cd17537      5 VVDDDEAVRDSLAFLLRSVGLAVKTftsASAFLAAAPP---DQPGCLVLDVRMPGMSGLELQDELLARGS--NIPIIFIT 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17537     80 GHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIE 113
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1062-1168 4.57e-13

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: 67.01  E-value: 4.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRP-----------DIVLTDLEMPRMNGIELAGHIRARPEY 1130
Cdd:cd17581      2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEedssnfnepkvNMIITDYCMPGMTGYDLLKKVKESSAL 81
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2047656081 1131 GRLPIVMITSRTT-QRHRKlAAEAGIDAYLTKPVRDDDL 1168
Cdd:cd17581     82 KEIPVVIMSSENIpTRISR-CLEEGAEDFLLKPVKLADV 119
ompR PRK09468
osmolarity response regulator; Provisional
1062-1176 7.72e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 69.62  E-value: 7.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGhiRARPEYGRLPIVMITSR 1141
Cdd:PRK09468     9 LVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICR--RLRSQNNPTPIIMLTAK 86
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK09468    87 GEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVL 121
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
1062-1162 1.15e-12

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: 65.30  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeyGRLPIVMITSR 1141
Cdd:cd17621      2 LVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR---SNVPVIMVTAK 78
                           90       100
                   ....*....|....*....|.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd17621     79 DSEIDKVVGLELGADDYVTKP 99
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
1061-1162 1.36e-12

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 64.87  E-value: 1.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITS 1140
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQR--LPQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1062-1176 2.11e-12

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: 64.88  E-value: 2.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDV-GYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITS 1140
Cdd:cd17552      5 LVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILLTA 84
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17552     85 KAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLL 120
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1064-1162 2.47e-12

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: 64.31  E-value: 2.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1064 VDDSLSNRRALEQLLGDVGYRVQTARDGVEA-TELLGRvRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSRT 1142
Cdd:cd17602      4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRAlTTLLNS-KPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKD 82
                           90       100
                   ....*....|....*....|
gi 2047656081 1143 TQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd17602     83 GLVDRIRAKMAGASGYLTKP 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1062-1113 4.61e-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: 61.82  E-value: 4.61e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMP 1113
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK15347 PRK15347
two component system sensor kinase;
1053-1163 5.41e-12

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 70.44  E-value: 5.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1053 EPASGLPLA------LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRA 1126
Cdd:PRK15347   679 EPVINLPLQpwqlqiLLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRD 758
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 2047656081 1127 RPEY--GRLPIVMITSRTTQRHRKLAAEAGIDAYLTKPV 1163
Cdd:PRK15347   759 DPNNldPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPV 797
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
1063-1163 5.41e-12

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 63.45  E-value: 5.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLL--GDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMITS 1140
Cdd:cd17565      3 IVDDDKNIIKILSDIIedDDLGEVVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGK--FIMISQ 80
                           90       100
                   ....*....|....*....|...
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPV 1163
Cdd:cd17565     81 VSDKEMIGKAYQAGIEFFINKPI 103
PRK15479 PRK15479
transcriptional regulator TctD;
1062-1183 7.30e-12

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 66.28  E-value: 7.30e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:PRK15479     4 LLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQ--TLPVLLLTAR 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLETGLALP 1183
Cdd:PRK15479    82 SAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQV 123
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1063-1162 1.47e-11

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: 62.08  E-value: 1.47e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSRT 1142
Cdd:cd19936      3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST---LPVIFLTSKD 79
                           90       100
                   ....*....|....*....|
gi 2047656081 1143 TQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19936     80 DEIDEVFGLRMGADDYITKP 99
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1062-1179 2.24e-11

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: 62.22  E-value: 2.24e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSR 1141
Cdd:cd17572      2 LLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQER--SLPTSVIVITAH 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2047656081 1142 TTQrhrKLAAEA---GIDAYLTKPVRDDDLLDRIRGLLETG 1179
Cdd:cd17572     80 GSV---DIAVEAmrlGAYDFLEKPFDADRLRVTVRNALKHR 117
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1062-1176 2.69e-11

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: 61.53  E-value: 2.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeyGRLPIVMITSR 1141
Cdd:cd18159      2 LIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQI---SNVPIIFISSR 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd18159     79 DDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1062-1172 3.12e-11

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: 61.65  E-value: 3.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPD--IVLTDLEMPRMNGIELAGHIRA-RPEYGRLPIVMI 1138
Cdd:cd19933      4 LLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKlFGRRERPLIVAL 83
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd19933     84 TANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10693 PRK10693
two-component system response regulator RssB;
1088-1173 4.48e-11

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 65.40  E-value: 4.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1088 ARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMI--TSRTTQRHRKLaaEAGIDAYLTKPVRD 1165
Cdd:PRK10693     3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGD--QTPVLVIsaTENMADIAKAL--RLGVQDVLLKPVKD 78

                   ....*...
gi 2047656081 1166 ddlLDRIR 1173
Cdd:PRK10693    79 ---LNRLR 83
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1062-1165 4.49e-11

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: 61.06  E-value: 4.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRAR-PEygrLPIVMITS 1140
Cdd:cd17555      4 LVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKEsPD---TPVIVVSG 80
                           90       100
                   ....*....|....*....|....*
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRD 1165
Cdd:cd17555     81 AGVMSDAVEALRLGAWDYLTKPIED 105
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
763-901 5.46e-11

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: 60.46  E-value: 5.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  763 ADPLMHLLRNAVDHGLESpeeravlgKPQAGRIVIAFEReGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRE 842
Cdd:pfam02518    3 ELRLRQVLSNLLDNALKH--------AAKAGEITVTLSE-GGELTLTVEDNGIGI----------------------PPE 51
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2047656081  843 LSELILRPnFSTRERaTQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLP 901
Cdd:pfam02518   52 DLPRIFEP-FSTADK-RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1062-1172 5.79e-11

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: 60.72  E-value: 5.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDV-GYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMIT 1139
Cdd:cd19925      4 LIVEDDPMVAEIHRAYVEQVpGFTViGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVD--VIVVT 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd19925     82 AANDVETVREALRLGVVDYLIKPFTFERLRQRL 114
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1061-1173 8.41e-11

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: 60.24  E-value: 8.41e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYR--VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMI 1138
Cdd:cd17532      1 ALIVDDEPLAREELRYLLEEHPDIeiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAK--PPLIVFV 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2047656081 1139 TSrttqrHRKLAAEA----GIDaYLTKPVRDDDL---LDRIR 1173
Cdd:cd17532     79 TA-----YDEYAVEAfelnAVD-YLLKPFSEERLaeaLAKLR 114
PRK15115 PRK15115
response regulator GlrR; Provisional
1062-1177 9.22e-11

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 65.63  E-value: 9.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:PRK15115     9 LLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQP--GMPVIILTAH 86
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:PRK15115    87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALE 122
PLN03029 PLN03029
type-a response regulator protein; Provisional
1062-1173 9.33e-11

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 63.13  E-value: 9.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLG-----RVRPDI---------------VLTDLEMPRMNGIELA 1121
Cdd:PLN03029    12 LAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGlheddRSNPDTpsvspnshqevevnlIITDYCMPGMTGYDLL 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2047656081 1122 GHIRARPEYGRLPIVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDlLDRIR 1173
Cdd:PLN03029    92 KKIKESSSLRNIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSD-LNRLK 142
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1062-1163 1.10e-10

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 59.67  E-value: 1.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRV-RPDIVLTDLEMPR-MNGIELAGhiRARPEYGRLPIVMIT 1139
Cdd:cd18161      2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAE--EARRRRPDLKVLLTS 79
                           90       100
                   ....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDaYLTKPV 1163
Cdd:cd18161     80 GYAENAIEGGDLAPGVD-VLSKPF 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1061-1176 1.17e-10

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 60.08  E-value: 1.17e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRArpeYGRLPIVMITS 1140
Cdd:cd17622      3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRP---KYQGPILLLTA 79
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1062-1173 1.19e-10

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 62.74  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLG-DVGYR-VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMIT 1139
Cdd:PRK10651    10 LLIDDHPMLRTGVKQLISmAPDITvVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR--IVVFS 87
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:PRK10651    88 VSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQ 121
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1062-1173 1.30e-10

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: 59.88  E-value: 1.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMITSR 1141
Cdd:cd17553      4 LIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIR--VIIMTAY 81
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd17553     82 GELDMIQESKELGALTHFAKPFDIDEIRDAVK 113
PRK10816 PRK10816
two-component system response regulator PhoP;
1062-1181 1.59e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 62.45  E-value: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGhiRARPEYGRLPIVMITSR 1141
Cdd:PRK10816     4 LVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIR--RWRSNDVSLPILVLTAR 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLE--TGLA 1181
Cdd:PRK10816    82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRrnSGLA 123
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1062-1162 1.64e-10

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: 58.99  E-value: 1.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeyGR-LPIVMITS 1140
Cdd:cd19935      2 LVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAA---GKqTPVLMLTA 78
                           90       100
                   ....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19935     79 RDSVEDRVKGLDLGADDYLVKP 100
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1062-1176 2.81e-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: 2.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygrLPIVMITSR 1141
Cdd:cd19938      3 LIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD---VPIIMVTAR 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd19938     80 VEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1063-1162 3.48e-10

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: 58.44  E-value: 3.48e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSrt 1142
Cdd:cd19919      5 IVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQR--HPDLPVIIMTA-- 80
                           90       100
                   ....*....|....*....|....*
gi 2047656081 1143 tqrHRKL-----AAEAGIDAYLTKP 1162
Cdd:cd19919     81 ---HSDLdsavsAYQGGAFEYLPKP 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
666-901 4.85e-10

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 61.56  E-value: 4.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  666 ELH-TASRRLVEAAVDAREIGLDIGKELDALNETLGQQELLALDTQEAV------MRTRLLTAESLLPRLQRSLRQTCRA 738
Cdd:COG4585     60 ELHdGVGQSLSAIKLQLEAARRLLDADPEAAREELEEIRELAREALAELrrlvrgLRPPALDDLGLAAALEELAERLLRA 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  739 TGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVDHGlespeeravlgkpQAGRIVIAFEREGGQVRVHCQDDGRGLD 818
Cdd:COG4585    140 AGIRVELDVDGDPDRLPPEVELALYRIVQEALTNALKHA-------------GATRVTVTLEVDDGELTLTVRDDGVGFD 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  819 LGAIhatavkrgllepgqaatprelselilrpnfstreratqtSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRI 898
Cdd:COG4585    207 PEAA---------------------------------------PGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATL 247

                   ...
gi 2047656081  899 PLP 901
Cdd:COG4585    248 PLA 250
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
1059-1176 4.92e-10

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 61.24  E-value: 4.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDslsnRRALEQLLGD----VGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRarpEYGRLP 1134
Cdd:PRK10710    11 PRILIVED----EPKLGQLLIDylqaASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---RFSDIP 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2047656081 1135 IVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK10710    84 IVMVTAKIEEIDRLLGLEIGADDYICKPYSPREVVARVKTIL 125
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
688-901 7.81e-10

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 61.85  E-value: 7.81e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  688 IGKELDALNETLGQQELLA-LDTQEAVMRTRLLTAESLLPRLQRSLRQtcRATGKQAGLTLAgggmlLDGDTLEALADP- 765
Cdd:COG0642    150 ILRSADRLLRLINDLLDLSrLEAGKLELEPEPVDLAELLEEVVELFRP--LAEEKGIELELD-----LPDDLPTVRGDPd 222
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  766 -----LMHLLRNAVDHGlespeeravlgkPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatP 840
Cdd:COG0642    223 rlrqvLLNLLSNAIKYT------------PEGGTVTVSVRREGDRVRISVEDTGPGI----------------------P 268
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2047656081  841 RELSELILRPnFSTRERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLP 901
Cdd:COG0642    269 PEDLERIFEP-FFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLPLA 328
fixJ PRK09390
response regulator FixJ; Provisional
1063-1178 1.12e-09

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 59.25  E-value: 1.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPeyGRLPIVMITSrt 1142
Cdd:PRK09390     8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARG--SPLPVIVMTG-- 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2047656081 1143 tqrHRK--LAAEA---GIDAYLTKPVRDDDLLDRIRGLLET 1178
Cdd:PRK09390    84 ---HGDvpLAVEAmklGAVDFIEKPFEDERLIGAIERALAQ 121
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
1062-1173 1.27e-09

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: 56.97  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLG-DVGYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMIT 1139
Cdd:cd19931      2 LLIDDHPLLRKGIKQLIElDPDFTVvGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSAR--IVILT 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:cd19931     80 VSDAEDDVVTALRAGADGYLLKDMEPEDLLEALK 113
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
1062-1176 1.31e-09

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 59.73  E-value: 1.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSR 1141
Cdd:PRK10161     6 LVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTAR 85
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK10161    86 GEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1062-1124 1.57e-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: 57.21  E-value: 1.57e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDV-GYRVQ-TARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHI 1124
Cdd:COG2197      5 LIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1071-1177 1.64e-09

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 56.51  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1071 RRALEQLLG--DVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMITSRTTQRHRK 1148
Cdd:cd19930     11 RGALAALLEleDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTK--VLIVTTFGRPGYFR 88
                           90       100
                   ....*....|....*....|....*....
gi 2047656081 1149 LAAEAGIDAYLTKPVRDDDLLDRIRGLLE 1177
Cdd:cd19930     89 RALAAGVDGYVLKDRPIEELADAIRTVHA 117
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
421-514 2.40e-09

Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 55.47  E-value: 2.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  421 QLLDILLQELPlhtRQFAESAQRLGAGGGLHDLETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSAcSKEGRMPGPAL 500
Cdd:cd00088      3 ELLELFLEEAE---ELLEELERALLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDA-LRDGLEVTPEL 78
                           90
                   ....*....|....
gi 2047656081  501 ARTLLDAADCLEAM 514
Cdd:cd00088     79 IDLLLDALDALKAE 92
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1062-1173 2.43e-09

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 60.28  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLL-GDVGYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHI-RARPeygrLPIVMI 1138
Cdd:PRK12555     4 GIVNDSPLAVEALRRALaRDPDHEVvWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRImAERP----CPILIV 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2047656081 1139 TSRTTQRHRKL--AAEAG-IDAyLTKPVRD---------DDLLDRIR 1173
Cdd:PRK12555    80 TSLTERNASRVfeAMGAGaLDA-VDTPTLGigagleeyaAELLAKID 125
PRK11173 PRK11173
two-component response regulator; Provisional
1059-1176 3.18e-09

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 58.87  E-value: 3.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRarpEYGRLPIVMI 1138
Cdd:PRK11173     4 PHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR---EQANVALMFL 80
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK11173    81 TGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLL 118
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1062-1169 3.40e-09

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 55.53  E-value: 3.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMIT-- 1139
Cdd:cd17563      4 LLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDAR--IVVLTgy 81
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 -SRTTqrhrklAAEA---GIDAYLTKPVRDDDLL 1169
Cdd:cd17563     82 aSIAT------AVEAiklGADDYLAKPADADEIL 109
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1062-1176 3.64e-09

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: 55.49  E-value: 3.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:cd17616      2 LLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKV--KTPILILSGL 79
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:cd17616     80 ADIEDKVKGLGFGADDYMTKPFHKDELVARIHAIV 114
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
725-900 3.80e-09

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 58.38  E-value: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  725 LPRLQRSLRQTCRATGKQAGLTLAgggMLLDGDTLEALADP------LMHLLRNAVDHGlespeeravlgkPQAGRIVIA 798
Cdd:COG2205     93 LAELLEEAVEELRPLAEEKGIRLE---LDLPPELPLVYADPelleqvLANLLDNAIKYS------------PPGGTITIS 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  799 FEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRELSELILRPnFSTRERATQTSGRGVGMDAVRARVIAL 878
Cdd:COG2205    158 ARREGDGVRISVSDNGPGI----------------------PEEELERIFER-FYRGDNSRGEGGTGLGLAIVKRIVEAH 214
                          170       180
                   ....*....|....*....|..
gi 2047656081  879 GGSLALDSTPGAGLGVELRIPL 900
Cdd:COG2205    215 GGTIWVESEPGGGTTFTVTLPL 236
CheW smart00260
Two component signalling adaptor domain;
943-1031 4.23e-09

Two component signalling adaptor domain;


Pssm-ID: 214588 [Multi-domain]  Cd Length: 138  Bit Score: 56.10  E-value: 4.23e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081   943 RLDGLDYPAATLRGLLRVPRRPDgDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGP----YLAKPPGVIGATVLGD 1018
Cdd:smart00260   47 NLRGEVLPVVDLRRLLGLPPEPP-TDETRVIVVETGDRKVGLVVDSVLGVREVVVKSIEPpppvSLSNAPGISGATILGD 125
                            90
                    ....*....|...
gi 2047656081  1019 GAVVPVIDLPELL 1031
Cdd:smart00260  126 GRVVLILDVDKLL 138
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
1062-1162 5.78e-09

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: 54.43  E-value: 5.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHI-RARPEygrLPIVMITS 1140
Cdd:cd19928      2 LVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDLIPRIkKARPD---LPIIVMSA 78
                           90       100
                   ....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd19928     79 QNTLMTAVKAAERGAFEYLPKP 100
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1062-1141 7.31e-09

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: 54.33  E-value: 7.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRP--DIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMIT 1139
Cdd:cd17582      2 LLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMMS 81

                   ..
gi 2047656081 1140 SR 1141
Cdd:cd17582     82 SQ 83
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
1062-1183 8.51e-09

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 60.13  E-value: 8.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRArpEYGRLPIVMITSR 1141
Cdd:PRK09959   962 LIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLRE--QNSSLPIWGLTAN 1039
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLETGLALP 1183
Cdd:PRK09959  1040 AQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIAP 1081
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1062-1162 1.21e-08

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: 53.66  E-value: 1.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRP-DIVLTDLEMPRMNGIELAghIRARPEYGRLPIVMITS 1140
Cdd:cd18160      3 LLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELA--REARKIDPDVKILFISG 80
                           90       100
                   ....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd18160     81 GAAAAPELLSDAVGDNATLKKP 102
PRK13557 PRK13557
histidine kinase; Provisional
1062-1181 1.30e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 58.91  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELL-GRVRPDIVLTDLEMP-RMNGIELAGHIRARpeYGRLPIVMIT 1139
Cdd:PRK13557   419 LIVDDRPDVAELARMILEDFGYRTLVASNGREALEILdSHPEVDLLFTDLIMPgGMNGVMLAREARRR--QPKIKVLLTT 496
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2047656081 1140 ---SRTTQRHRKLAAEAGIdayLTKPVRDDDLLDRIRGLLE--TGLA 1181
Cdd:PRK13557   497 gyaEASIERTDAGGSEFDI---LNKPYRRAELARRVRMVLDgpTGVG 540
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
1062-1179 1.33e-08

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 56.86  E-value: 1.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITSR 1141
Cdd:PRK09836     4 LIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANK--GMPILLLTAL 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLETG 1179
Cdd:PRK09836    82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRG 119
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
1062-1173 1.53e-08

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 56.35  E-value: 1.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTA----RDGVEAtellGRVRPDIVLTDLEMPRMNGIELaghIRARPEYGRLPIVM 1137
Cdd:PRK10529     5 LIVEDEQAIRRFLRTALEGDGMRVFEAetlqRGLLEA----ATRKPDLIILDLGLPDGDGIEF---IRDLRQWSAIPVIV 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1138 ITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:PRK10529    78 LSARSEESDKIAALDAGADDYLSKPFGIGELQARLR 113
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
1085-1162 2.37e-08

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


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 53.00  E-value: 2.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1085 VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITS----RTTQRhrklAAEAGIDAYLT 1160
Cdd:cd17561     30 VGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLTAfgqeDITQR----AVELGASYYIL 105

                   ..
gi 2047656081 1161 KP 1162
Cdd:cd17561    106 KP 107
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1062-1170 2.64e-08

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: 53.31  E-value: 2.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLL-GDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMITS 1140
Cdd:cd17593      4 LICDDSSMARKQLARALpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQL--ETKVIVVSG 81
                           90       100       110
                   ....*....|....*....|....*....|
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLD 1170
Cdd:cd17593     82 DVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
CheW pfam01584
CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. ...
908-1030 2.85e-08

CheW-like domain; CheW proteins are part of the chemotaxis signaling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 460257 [Multi-domain]  Cd Length: 131  Bit Score: 53.36  E-value: 2.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  908 LLAQVGPHRVAIVNKGLEQIRHRDDAEP-GGDPAW----ARLDGLDYPAATLRGLLRVPRRPDGDgRGVLLLARAADGAT 982
Cdd:pfam01584    2 LLFRLGGETFAIPISKVREILRPPPITPiPGAPGYvlgvINLRGEVLPVIDLRRLLGLPPTEPRE-RTRVVVVEVGGQVV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2047656081  983 AVWVDALLDSWDVVVKPLGPYLA---KPPGVIGATVLGDGAVVPVIDLPEL 1030
Cdd:pfam01584   81 GLLVDEVIGVLEIVIKQIEPPLGlgrVAGYISGATILGDGRVVLILDVEAL 131
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
769-900 3.50e-08

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 57.17  E-value: 3.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  769 LLRNAVDHGLESPEERavlgkpqaGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRELSELIL 848
Cdd:COG3290    289 LLDNAIEAVEKLPEEE--------RRVELSIRDDGDELVIEVEDSGPGI----------------------PEELLEKIF 338
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  849 RPNFSTRERAtqtsGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPL 900
Cdd:COG3290    339 ERGFSTKLGE----GRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPK 386
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
421-509 4.10e-08

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072).


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 51.58  E-value: 4.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  421 QLLDILLQELPlhtrqfaESAQRLGAGGGLHDLETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSACSKEGRMPGPAL 500
Cdd:pfam01627    1 ELLELFLEEAP-------ELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLDPELLEA 73

                   ....*....
gi 2047656081  501 ARTLLDAAD 509
Cdd:pfam01627   74 LRDLLEALR 82
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
1061-1161 5.33e-08

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 54.52  E-value: 5.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGYRVQTA-RDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGrlPIVMIT 1139
Cdd:PRK09958     3 AIIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSG--IIIIVS 80
                           90       100
                   ....*....|....*....|..
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTK 1161
Cdd:PRK09958    81 AKNDHFYGKHCADAGANGFVSK 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
769-900 6.23e-08

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 56.56  E-value: 6.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  769 LLRNAVDHGLESpeeravlgKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGAIHAtavkrgllepgqaatprelseliL 848
Cdd:COG2972    344 LVENAIEHGIEP--------KEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEK-----------------------L 392
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2047656081  849 RPNFSTRERatqtsGRGVGMDAVRARVIAL---GGSLALDSTPGAGLGVELRIPL 900
Cdd:COG2972    393 LEELSSKGE-----GRGIGLRNVRERLKLYygeEYGLEIESEPGEGTTVTIRIPL 442
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1062-1181 6.45e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 56.58  E-value: 6.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRA-RPEygrLPIVMITS 1140
Cdd:PRK10365     9 LVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAlNPA---IPVLIMTA 85
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRdddlLDRIRGLLETGLA 1181
Cdd:PRK10365    86 YSSVETAVEALKTGALDYLIKPLD----FDNLQATLEKALA 122
CheW_like cd00588
CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. ...
907-1030 8.34e-08

CheW-like domain. CheW proteins are part of the chemotaxis signalling mechanism in bacteria. CheW interacts with the methyl accepting chemotaxis proteins (MCPs) and relays signals to CheY, which affects flageller rotation. This family includes CheW and other related proteins that are involved in chemotaxis. The CheW-like regulatory domain in the chemotaxis associated histidine kinase CheA binds to CheW, suggesting that these domains can interact with each other.


Pssm-ID: 238331  Cd Length: 136  Bit Score: 52.28  E-value: 8.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  907 ALLAQVGPHRVAI-VNKGLEQIRHRDDAEPGGDPAWAR----LDGLDYPAATLRGLLRVPRRPDGDGRGVLLLARAADGA 981
Cdd:cd00588      4 VLLFRVGDELYAIpIAVVEEILPLPPITRVPNAPDYVLgvinLRGEILPVIDLRRLFGLEAAEPDTDETRIVVVEVGDRK 83
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2047656081  982 TAVWVDALLDSWDVVVKPLGPYL----AKPPGVIGATVLGDGAVVPVIDLPEL 1030
Cdd:cd00588     84 VGLVVDSVLGVLEVVIKDIEPPPdvgsSNAPGISGATILGDGRVVLILDVDKL 136
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
688-900 9.67e-08

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: 55.74  E-value: 9.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  688 IGKELDALNETLgqQELLALdtqeAVMRTRLLTAESLlPRLQRSLRQTCRATGKQAGLTLAgggMLLDGDTLEALADP-- 765
Cdd:COG5000    248 IIRQVDRLKRIV--DEFLDF----ARLPEPQLEPVDL-NELLREVLALYEPALKEKDIRLE---LDLDPDLPEVLADRdq 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  766 ----LMHLLRNAVDhglespeerAVlgkPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPR 841
Cdd:COG5000    318 leqvLINLLKNAIE---------AI---EEGGEIEVSTRREDGRVRIEVSDNGPGI----------------------PE 363
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2047656081  842 ELSELILRPNFSTREratqtSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPL 900
Cdd:COG5000    364 EVLERIFEPFFTTKP-----KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPL 417
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
1053-1172 3.48e-07

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 54.86  E-value: 3.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1053 EPASGLPLA-LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYG 1131
Cdd:PRK11107   661 TDESRLPLTvMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQ 740
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2047656081 1132 RLPIVMITSRTT--QRHRKLAaeAGIDAYLTKPVrDDDLLDRI 1172
Cdd:PRK11107   741 NTPIIAVTAHAMagERERLLS--AGMDDYLAKPI-DEAMLKQV 780
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
1062-1173 3.97e-07

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 52.16  E-value: 3.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLG-DVGYRV-QTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRlpIVMIT 1139
Cdd:PRK10403    10 LIVDDHPLMRRGVRQLLElDPGFEVvAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQ--IIILT 87
                           90       100       110
                   ....*....|....*....|....*....|....
gi 2047656081 1140 SRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:PRK10403    88 VSDASSDVFALIDAGADGYLLKDSDPEVLLEAIR 121
PRK10643 PRK10643
two-component system response regulator PmrA;
1062-1176 6.24e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 51.57  E-value: 6.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRaRPEYGrLPIVMITSR 1141
Cdd:PRK10643     4 LIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWR-QKKYT-LPVLILTAR 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK10643    82 DTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
1061-1172 6.56e-07

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 49.18  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLLGDVGY-RVQTARDGVEATELLGRVRPDIVLTDLEM-PRMNGIELAGHIRarpEYGRLP---- 1134
Cdd:cd17589      1 FLIVDDQPTFRSMLKSMLRSLGVtRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELR---HKKLISpstv 77
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2047656081 1135 IVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd17589     78 FIMVTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1062-1163 8.38e-07

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: 48.98  E-value: 8.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGY-RVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIrARPEYGRLPIVM--I 1138
Cdd:cd17530      4 LVLDDDPFQCMMAATILEDLGPgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHL-AESHSNAAVILMsgL 82
                           90       100
                   ....*....|....*....|....*..
gi 2047656081 1139 TSRTTQRHRKLAAEAGID--AYLTKPV 1163
Cdd:cd17530     83 DGGILESAETLAGANGLNllGTLSKPF 109
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1063-1167 1.71e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 52.18  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1063 VVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITSRT 1142
Cdd:PRK10923     8 VVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQR--HPMLPVIIMTAHS 85
                           90       100
                   ....*....|....*....|....*
gi 2047656081 1143 TQRHRKLAAEAGIDAYLTKPVRDDD 1167
Cdd:PRK10923    86 DLDAAVSAYQQGAFDYLPKPFDIDE 110
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
1062-1172 2.50e-06

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: 47.43  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTArDGVEATELLGRVRP-DIVLTDLEMPRMNGIELAGHIRARpeYGRLPIVMITS 1140
Cdd:cd17573      2 LLIEDDSTLGKEISKGLNEKGYQADVA-ESLKDGEYYIDIRNyDLVLVSDKLPDGNGLSIVSRIKEK--HPSIVVIVLSD 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRI 1172
Cdd:cd17573     79 NPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
217-779 5.74e-06

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 51.03  E-value: 5.74e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  217 ATLEALLTEDAHTAAAASWPPPLRQDAPDRAA-LDAL----------------PGAARELIELLLMQVCATDAELHRAGI 279
Cdd:COG3321    801 PVLTGLVRQCLAAAGDAVVLPSLRRGEDELAQlLTALaqlwvagvpvdwsalyPGRGRRRVPLPTYPFQREDAAAALLAA 880
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  280 SGTAEDLAQARETLECLGSAAEAAGFGGLARLCGHCGANLQRFLDDAPAADPARLRLPREWLARVAGYLPQSTAPDAGRG 359
Cdd:COG3321    881 ALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAE 960
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  360 VVAYLQDPAWPLPLPAATAADILERMDGGDLREIRGESTPTRPQTATAEDVSLAP-----PPDVNPQLLDILLQELPLHT 434
Cdd:COG3321    961 AGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAaaaaaLLALAALLAAAAAALAAAAA 1040
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  435 RQFAESAQRLGAGGGLHDLETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILSACSKEGRMPGPALARTLLDAADCLEAM 514
Cdd:COG3321   1041 AAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAA 1120
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  515 GEALQGRGTPPAEARTVLQEVLDWANRIDRDGLSALDAPDAPAPAHPADTQDGAPAPPAPQDTPGTSTVRVPTAWIESLL 594
Cdd:COG3321   1121 AAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAAL 1200
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  595 RLSGESLVHSAQAHERLRRIKIQLQAMRAQFESLQGLGAELEELIDVRDWSGPAGGTGGQDFDNLEMDQYNELHTASRRL 674
Cdd:COG3321   1201 LAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAA 1280
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  675 VEAAVDAREIGLDIGKELDALNETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGKQAGLTLAGGGMLL 754
Cdd:COG3321   1281 AAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAA 1360
                          570       580
                   ....*....|....*....|....*
gi 2047656081  755 DGDTLEALADPLMHLLRNAVDHGLE 779
Cdd:COG3321   1361 AALAAAAGAAAAAAALALAALAAAV 1385
PRK11697 PRK11697
two-component system response regulator BtsR;
1061-1173 8.46e-06

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 48.30  E-value: 8.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1061 ALVVDDSLSNRRALEQLL---GDVGYrVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIraRPEygRLP-IV 1136
Cdd:PRK11697     4 VLIVDDEPLAREELRELLqeeGDIEI-VGECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGML--DPE--HMPyIV 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2047656081 1137 MITSrttqrHRKLAAEA----GIDaYLTKPVRDDDL---LDRIR 1173
Cdd:PRK11697    79 FVTA-----FDEYAIKAfeehAFD-YLLKPIDPARLaktLARLR 116
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
1090-1173 1.04e-05

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 46.25  E-value: 1.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1090 DGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGRLPIVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLL 1169
Cdd:cd17575     33 DPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVLSTKEEPEVKSEAFALGANDYLVKLPDKIELV 112

                   ....
gi 2047656081 1170 DRIR 1173
Cdd:cd17575    113 ARIR 116
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
754-900 1.28e-05

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 49.03  E-value: 1.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  754 LDGDTLEALADP------LMHLLRNAVDhglespeerAVLGKPQaGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatav 827
Cdd:COG4191    243 LPPDLPPVLGDPgqleqvLLNLLINAID---------AMEEGEG-GRITISTRREGDYVVISVRDNGPGI---------- 302
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2047656081  828 krgllepgqaatPRELSELILRPNFSTREratQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPL 900
Cdd:COG4191    303 ------------PPEVLERIFEPFFTTKP---VGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
PRK15369 PRK15369
two component system response regulator;
1085-1161 1.50e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 47.38  E-value: 1.50e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047656081 1085 VQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRAR-PEygrLPIVMITSRTTQRHRKLAAEAGIDAYLTK 1161
Cdd:PRK15369    32 VGQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRwPA---MNILVLTARQEEHMASRTLAAGALGYVLK 106
PRK13856 PRK13856
two-component response regulator VirG; Provisional
1062-1173 1.93e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 47.50  E-value: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELaghIRARPEYGRLPIVMIT-S 1140
Cdd:PRK13856     5 LVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEI---VRSLATKSDVPIIIISgD 81
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2047656081 1141 RTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:PRK13856    82 RLEEADKVVALELGATDFIAKPFGTREFLARIR 114
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1059-1176 2.23e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 47.26  E-value: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEygRLPIVMI 1138
Cdd:PRK11083     4 PTILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHP--ALPVIFL 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK11083    82 TARSDEVDRLVGLEIGADDYVAKPFSPREVAARVRTIL 119
PRK11517 PRK11517
DNA-binding response regulator HprR;
1062-1176 2.70e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 46.82  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNGIELaghIRARPEYGRLPIVMITSR 1141
Cdd:PRK11517     4 LLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQI---LQTLRTAKQTPVICLTAR 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1142 TTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLL 1176
Cdd:PRK11517    81 DSVDDRVRGLDSGANDYLVKPFSFSELLARVRAQL 115
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
769-899 6.05e-05

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: 43.43  E-value: 6.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  769 LLRNAVDhglespeerAVLGKPQAGRIV-IAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRELSELI 847
Cdd:cd16915      8 LIDNALD---------ALAATGAPNKQVeVFLRDEGDDLVIEVRDTGPGI----------------------APELRDKV 56
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2047656081  848 LRPNFSTREratqTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIP 899
Cdd:cd16915     57 FERGVSTKG----QGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK09483 PRK09483
response regulator; Provisional
1062-1173 6.58e-05

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 45.48  E-value: 6.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1062 LVVDDSLSNRRALEQLLGDV-GYRVQ-TARDGVEATELLGRVRPDIVLTDLEMPRMNGIELAGHI-RARPEygrLPIVMI 1138
Cdd:PRK09483     5 LLVDDHELVRAGIRRILEDIkGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKIlRYTPD---VKIIML 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2047656081 1139 TSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIR 1173
Cdd:PRK09483    82 TVHTENPLPAKVMQAGAAGYLSKGAAPQEVVSAIR 116
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
421-506 1.16e-04

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates phosphotransfer reactions. Domain detected only in eubacteria. This alignment is an extension to that shown in the Cell structure paper.


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 42.24  E-value: 1.16e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081   421 QLLDILLQELPLHTRQFAESAQRLGAGGGLHDLETAQRLAHTLKGSANTVGIVGVAQLTHHLEDILsacsKEGRMPGPAL 500
Cdd:smart00073    1 GGLELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLL----DALRSGEVEL 76

                    ....*.
gi 2047656081   501 ARTLLD 506
Cdd:smart00073   77 TPDLLD 82
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
536-1094 1.80e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 46.02  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  536 LDWANRIDRDGLSAldapdapapahpadtqdgAPAPPAPQDTPGTSTVRVPTAWIESLLRLSGESLVHSAQAHERLRRIK 615
Cdd:COG3321    847 VDWSALYPGRGRRR------------------VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAAL 908
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  616 IQLQAMRAQFESLQGLGAELEELIDVRDWSGPAGGTGGQDFDNLEMDQYNELHTASRRLVEAAvDAREIGLDIGKELDAL 695
Cdd:COG3321    909 LALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAA-AAAAAAAAAAAAAAAA 987
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  696 NETLGQQELLALDTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDGDTLEALADPLMHLLRNAVD 775
Cdd:COG3321    988 AAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAA 1067
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  776 HGLESPEERAVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLDLGAIHATAVKRGLLEPGQAATPRELSELILRPNFSTR 855
Cdd:COG3321   1068 LLLLAALAELALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAA 1147
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  856 ERATQTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLPLSRSLALLAQVGPHRVAIVNKGLEQIRHRDDAEP 935
Cdd:COG3321   1148 AALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAA 1227
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  936 GGDPAWARLDGLDYPAATLRGLLRVPRRPDGDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATV 1015
Cdd:COG3321   1228 AAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAA 1307
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2047656081 1016 LGDGAVVPVIDLPELLRGAAPGPAAAPWDGEAAARDGEPASGLPLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEA 1094
Cdd:COG3321   1308 AAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAVA 1386
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
798-1183 2.17e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 45.63  E-value: 2.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  798 AFEREGGQVRVHCQDDGRGLDLGAIHATAVKRGLLEPGQAATPRELSELILRPNFSTRERATQTSGRGVGMDAVRARVIA 877
Cdd:COG3321    867 PFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALA 946
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  878 LGGSLALDSTPGAGLGVELRIPLPLSRSLALLAQVGPHRVAIVNKGLEQIRHRDDAEPGGDPAWARLDGLDYPAATLRGL 957
Cdd:COG3321    947 AAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAA 1026
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  958 LRVPRRPDGDGRGVLLLARAADGATAVWVDALLDSWDVVVKPLGPYLAKPPGVIGATVLGDGAVVPVIDLPELLRGAAPG 1037
Cdd:COG3321   1027 LLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAALAAAL 1106
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1038 PAAAPWDGEAAARDGEPASGLPLALVVDDSLSNRRALEQLLGDVGYRVQTARDGVEATELLGRVRPDIVLTDLEMPRMNG 1117
Cdd:COG3321   1107 LLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALA 1186
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2047656081 1118 IELAGHIRARPEYGRLPIVMITSRTTQRHRKLAAEAGIDAYLTKPVRDDDLLDRIRGLLETGLALP 1183
Cdd:COG3321   1187 AALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAA 1252
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
1046-1163 2.28e-04

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 45.32  E-value: 2.28e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1046 EAAARDGEPASGLPLALVVDDSLS---NRRALEQLlgdvGYRVQTARDGVEAtelLGRVRP---DIVLTDLEMPRMNGIE 1119
Cdd:PRK11091   514 DAFDEDDMPLPALNILLVEDIELNvivARSVLEKL----GNSVDVAMTGKEA---LEMFDPdeyDLVLLDIQLPDMTGLD 586
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2047656081 1120 LAGHIRARPEYGRL-PIVMITSRTTQRHRKLaAEAGIDAYLTKPV 1163
Cdd:PRK11091   587 IARELRERYPREDLpPLVALTANVLKDKKEY-LDAGMDDVLSKPL 630
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
725-900 7.48e-04

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 43.39  E-value: 7.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  725 LPRLQRSLRQTCRATGKQAGLTLAgggMLLDGDTLEALADP------LMHLLRNAVDHGlespeeravlgkPQAGRIVIA 798
Cdd:COG5002    242 LAELLEEVVEELRPLAEEKGIELE---LDLPEDPLLVLGDPdrleqvLTNLLDNAIKYT------------PEGGTITVS 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  799 FEREGGQVRVHCQDDGRGLDlgaihatavkrgllepgqaatPRELsELILRPNFSTRE-RATQTSGRGVGMDAVRARVIA 877
Cdd:COG5002    307 LREEDDQVRISVRDTGIGIP---------------------EEDL-PRIFERFYRVDKsRSRETGGTGLGLAIVKHIVEA 364
                          170       180
                   ....*....|....*....|...
gi 2047656081  878 LGGSLALDSTPGAGLGVELRIPL 900
Cdd:COG5002    365 HGGRIWVESEPGKGTTFTITLPL 387
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
677-904 1.96e-03

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 42.08  E-value: 1.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  677 AAVDAREIGLDIGKELDALNETLgqQELLALdTQEAVMRTRLLTAESLLPRLQRSLRQTCRATGKQAGLTLAGGGMLLDG 756
Cdd:PRK10364   268 AGGEAHQLAQVMAKEADRLNRVV--SELLEL-VKPTHLALQAVDLNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQA 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  757 DTlEALADPLMHLLRNAVDhglespeeravlGKPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgq 836
Cdd:PRK10364   345 DP-DRLTQVLLNLYLNAIQ------------AIGQHGVISVTASESGAGVKISVTDSGKGI------------------- 392
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047656081  837 aaTPRELsELILRPNFSTRERATqtsgrGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIPLPLSR 904
Cdd:PRK10364   393 --AADQL-EAIFTPYFTTKAEGT-----GLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITR 452
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
795-901 2.45e-03

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: 38.58  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  795 IVIAFEREGGQVRVHCQDDGRGLDLGaihatavkrgLLEPGQAATPRELSELiLRPnFSTRERATQTSGRGVGMDAVRAR 874
Cdd:cd16950      9 VDNALRYGGGWVEVSSDGEGNRTRIQ----------VLDNGPGIAPEEVDEL-FQP-FYRGDNARGTSGTGLGLAIVQRI 76
                           90       100
                   ....*....|....*....|....*..
gi 2047656081  875 VIALGGSLALDSTPGAGLgvELRIPLP 901
Cdd:cd16950     77 SDAHGGSLTLANRAGGGL--CARIELP 101
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
769-899 3.09e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 41.44  E-value: 3.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  769 LLRNAVDhglespeerAVLGKPQaGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRELSELIL 848
Cdd:PRK11086   441 LIENALE---------AVGGEEG-GEISVSLHYRNGWLHCEVSDDGPGI----------------------APDEIDAIF 488
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2047656081  849 RPNFSTReratqTSGRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIP 899
Cdd:PRK11086   489 DKGYSTK-----GSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
1093-1177 3.16e-03

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; 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 AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 39.14  E-value: 3.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1093 EATELLGRVRPDIVLTDLEMPRMNGIELAGHIRARPEYGrlPIVMITSrttqrHRKLAA---EAGIDA--YLTKPVRDDD 1167
Cdd:cd17533     44 EKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDPYA--IIIFVTT-----HSEFAPltfEYKVAAldFILKPLKLEE 116
                           90
                   ....*....|
gi 2047656081 1168 LLDRIRGLLE 1177
Cdd:cd17533    117 FKKRIEECIK 126
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
1059-1162 3.17e-03

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.24  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081 1059 PLALVVDDSLSNRRALEQLL-----GDvgYRVQTARDGVEATELLG--RVRPDIV---LTDLEMPRMNGIELAGHIRA-R 1127
Cdd:cd17595      1 PIILTVDDDPQVLRAVARDLrrqygKD--YRVLRADSGAEALDALKelKLRGEAValfLVDQRMPEMDGVEFLEKAMElF 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2047656081 1128 PEYGRlpiVMITSRT-TQRHRKLAAEAGIDAYLTKP 1162
Cdd:cd17595     79 PEAKR---VLLTAYAdTDAAIRAINDVQLDYYLLKP 111
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
754-905 5.66e-03

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 40.60  E-value: 5.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  754 LDGDTLEALADP------LMHLLRNAVDHGlespeeravlgkPQAGRIVI----------AFEREGGQVRVHCQDDGRGL 817
Cdd:COG3852    231 YDPSLPEVLGDPdqliqvLLNLVRNAAEAM------------PEGGTITIrtrverqvtlGGLRPRLYVRIEVIDNGPGI 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  818 dlgaihatavkrgllepgqaatPRELSELILRPNFSTREratqtSGRGVGMdAVRARVI-ALGGSLALDSTPGAglGVEL 896
Cdd:COG3852    299 ----------------------PEEILDRIFEPFFTTKE-----KGTGLGL-AIVQKIVeQHGGTIEVESEPGK--GTTF 348

                   ....*....
gi 2047656081  897 RIPLPLSRS 905
Cdd:COG3852    349 RIYLPLEQA 357
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
754-818 5.94e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Erythrobacter litoralis blue light-activated histidine kinase 2; This domain family includes the histidine kinase-like ATPase (HATPase) domain of blue light-activated histidine kinase 2 of Erythrobacter litoralis (EL346). Signaling commonly occurs within HK dimers, however EL346 functions as a monomer. Also included in this family are the HATPase domains of ethanolamine utilization sensory transduction histidine kinase (EutW), whereby regulation of ethanolamine, a carbon and nitrogen source for gut bacteria, results in autophosphorylation and subsequent phosphoryl transfer to a response regulator (EutV) containing an RNA-binding domain. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory PAS sensor domain, while some have an N-terminal histidine kinase domain.


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 38.17  E-value: 5.94e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2047656081  754 LDGDTLEALADPLMHLLRNAVDHGLESPEEravlgkpqaGRIVIAFEREGGQVRVHCQDDGRGLD 818
Cdd:cd16951     32 VSSEVATAIGLVVNELLQNALKHAFSDREG---------GTITIRSVVDGDYLRITVIDDGVGLP 87
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
863-899 6.91e-03

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: 36.76  E-value: 6.91e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 2047656081  863 GRGVGMDAVRARVIALGGSLALDSTPGAGLGVELRIP 899
Cdd:cd16917     51 GGGFGLLGMRERAELLGGTLTIGSRPGGGTRVTARLP 87
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
1074-1139 7.51e-03

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 37.61  E-value: 7.51e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2047656081 1074 LEQLLGDVGYRVQ-TARDGVEATELLGRVRPDIVLTDLEMP-RMNGIELAGHIRarpEYGRLPIVMIT 1139
Cdd:cd17540     16 LEQIVEDLGHQVVgIARTRDEAVALARRERPDLILADIQLAdGSSGIDAVNEIL---TTHDVPVIFVT 80
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
766-891 7.70e-03

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: 37.05  E-value: 7.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2047656081  766 LMHLLRNAVDhglespeeraVLGKPQAGRIVIAFEREGGQVRVHCQDDGRGLdlgaihatavkrgllepgqaatPRELSE 845
Cdd:cd16976      5 LMNLLQNALD----------AMGKVENPRIRIAARRLGGRLVLVVRDNGPGI----------------------AEEHLS 52
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 2047656081  846 LILRPNFSTREratqtSGRGVGMD-AVRARVIA-LGGSLALDSTPGAG 891
Cdd:cd16976     53 RVFDPFFTTKP-----VGKGTGLGlSISYGIVEeHGGRLSVANEEGAG 95
 
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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