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Conserved domains on  [gi|2425845196|dbj|BDV44930|]
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hybrid sensor histidine kinase/response regulator [Geotalea uraniireducens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
114-509 4.67e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


:

Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.05  E-value: 4.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 114 RVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADI 193
Cdd:COG5002    22 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 194 PASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSatpLRNATGEMIGSVEILHDMSTLKALEQEREDFVSMLSHDLKT 273
Cdd:COG5002   102 LILLLLLALLILLAALLLLLSELLLLLLLLGRLSLR---LSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 274 PITAVVGSIDLVREGRLGTiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVA 353
Cdd:COG5002   179 PLTSIRGYLELLLDGAADD-PEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 354 LRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFL 433
Cdd:COG5002   258 EEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLR-----------------------EEDDQV 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196 434 LLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG5002   315 RISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-157 8.81e-46

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: 165.14  E-value: 8.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENeRLQRELDEQRQKMAAILRgMADMVVAVD 157
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRREN-AEDSGLIGRSPAMQEVRR-LIEKVAPSD 154
 
Name Accession Description Interval E-value
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
114-509 4.67e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.05  E-value: 4.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 114 RVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADI 193
Cdd:COG5002    22 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 194 PASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSatpLRNATGEMIGSVEILHDMSTLKALEQEREDFVSMLSHDLKT 273
Cdd:COG5002   102 LILLLLLALLILLAALLLLLSELLLLLLLLGRLSLR---LSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 274 PITAVVGSIDLVREGRLGTiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVA 353
Cdd:COG5002   179 PLTSIRGYLELLLDGAADD-PEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 354 LRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFL 433
Cdd:COG5002   258 EEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLR-----------------------EEDDQV 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196 434 LLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG5002   315 RISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-157 8.81e-46

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: 165.14  E-value: 8.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENeRLQRELDEQRQKMAAILRgMADMVVAVD 157
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRREN-AEDSGLIGRSPAMQEVRR-LIEKVAPSD 154
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
6-120 8.97e-40

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: 139.55  E-value: 8.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
145-509 3.63e-39

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 150.50  E-value: 3.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 145 ILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRlPCRVVLTTGEPCLDVTYVVAQGKRRL 224
Cdd:PRK11360  267 ILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFAS-PLLDTLEHGTEHVDLEISFPGRDRTI 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 225 PVLSSATPLRNATGEMIGSVEILHDMSTLKALE-----QER----EDFVSMLSHDLKTPITAVVGSIDLVREgrlGTINA 295
Cdd:PRK11360  346 ELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQrrvarQERlaalGELVAGVAHEIRNPLTAIRGYVQIWRQ---QTSDP 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 296 EQKEYLDSAVESCDEMVEMIDTLLDvhkFEAGRmQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDR 375
Cdd:PRK11360  423 PSQEYLSVVLREVDRLNKVIDQLLE---FSRPR-ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADP 498
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 376 SKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEplalagplsaaayppanlpvagRFLLLTVRDTGAGVPADCLVSIFDR 455
Cdd:PRK11360  499 ELLKQVLLNILINAVQAISARGKIRIRTWQYSD----------------------GQVAVSIEDNGCGIDPELLKKIFDP 556
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 456 FVQAKNRrqgktgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:PRK11360  557 FFTTKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQ 604
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
6-116 7.28e-36

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: 129.19  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
374-507 3.47e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 110.82  E-value: 3.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVaeplalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIF 453
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD-----------------------GDHVEITVEDNGPGIPPEDLEKIF 58
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196  454 DRFVQAKNRRQgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPME 507
Cdd:smart00387  59 EPFFRTDKRSR-KIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-174 5.50e-29

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 119.18  E-value: 5.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDEQRQ---------KMAAILRGMADMVVA 155
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQwghiltnspAMMDICKDTAKIALS 165
                         170       180
                  ....*....|....*....|.
gi 2425845196 156 vdrQGNVITL--NGKAEELLA 174
Cdd:PRK11361  166 ---QASVLISgeSGTGKELIA 183
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
382-506 1.17e-28

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


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 109.50  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTpEEGEIEIRAEIVAEPLALAGplsaaayppanlpvagrfLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:cd16922     5 LLNLLGNAIKFT-EEGEVTLRVSLEEEEEDGVQ------------------LRFSVEDTGIGIPEEQQARLFEPFSQADS 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2425845196 462 RRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPM 506
Cdd:cd16922    66 STTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
227-505 3.20e-25

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 108.24  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 227 LSSATPLRNATGEMIGSVEILHDMstLKALE---QEREDFVSMLSHDLKTPITAVVG--SIDLVREgrlgTINAEQKEYL 301
Cdd:TIGR01386 207 LDQRLDPSRAPAELRELAQSFNAM--LGRLEdafQRLSQFSADLAHELRTPLTNLLGqtQVALSQP----RTGEEYREVL 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 302 DSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHlppAPILFPVDRSKFFRL 381
Cdd:TIGR01386 281 ESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVE---GEGLVRGDPQMFRRA 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:TIGR01386 358 ISNLLSNALRHTPDGGTITVRIE-----------------------RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDP 414
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2425845196 462 RRQGKTGGSGLGLAFCRKAMDAHDGFVWAESeLDKGSSFHLLFP 505
Cdd:TIGR01386 415 ARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
374-508 6.27e-25

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: 98.98  E-value: 6.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpvAGRFLLLTVRDTGAGVPADCLVSIF 453
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLS------------------------EGGELTLTVEDNGIGIPPEDLPRIF 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2425845196 454 DRFVQAKNRrqgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMER 508
Cdd:pfam02518  58 EPFSTADKR---GGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
5-132 2.53e-20

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 89.70  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:TIGR02154   4 RILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRpeTRAIPIIMLT 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQ 132
Cdd:TIGR02154  84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIE 133
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-58 2.50e-13

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: 64.51  E-value: 2.50e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196    5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMP 58
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
 
Name Accession Description Interval E-value
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
114-509 4.67e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 229.05  E-value: 4.67e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 114 RVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADI 193
Cdd:COG5002    22 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLAL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 194 PASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSatpLRNATGEMIGSVEILHDMSTLKALEQEREDFVSMLSHDLKT 273
Cdd:COG5002   102 LILLLLLALLILLAALLLLLSELLLLLLLLGRLSLR---LSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 274 PITAVVGSIDLVREGRLGTiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVA 353
Cdd:COG5002   179 PLTSIRGYLELLLDGAADD-PEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 354 LRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFL 433
Cdd:COG5002   258 EEKGIELELDLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLR-----------------------EEDDQV 314
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196 434 LLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG5002   315 RISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
245-509 2.78e-68

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 219.01  E-value: 2.78e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 245 EILHDMSTLKALEQEREDFVSMLSHDLKTPITAVVGSIDLVREgRLGTINAEQKEYLDSAVESCDEMVEMIDTLLDVHKF 324
Cdd:COG2205     1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLD-EEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 325 EAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAE 404
Cdd:COG2205    80 ESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISAR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 405 ivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRqgKTGGSGLGLAFCRKAMDAH 484
Cdd:COG2205   160 -----------------------REGDGVRISVSDNGPGIPEEELERIFERFYRGDNSR--GEGGTGLGLAIVKRIVEAH 214
                         250       260
                  ....*....|....*....|....*
gi 2425845196 485 DGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG2205   215 GGTIWVESEPGGGTTFTVTLPLAES 239
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
169-507 7.64e-62

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 205.53  E-value: 7.64e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 169 AEELLAIRAEEVLGRPVEELLQADIPASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSATPLRNATGEMIGSVEILH 248
Cdd:COG0642    19 LLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 249 DMSTLKALEQEREDFVSMLSHDLKTPITAVVGSIDLVREgrlgTINAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGR 328
Cdd:COG0642    99 LLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE----ELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 329 MQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivae 408
Cdd:COG0642   175 LELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVR---- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 409 plalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGktGGSGLGLAFCRKAMDAHDGFV 488
Cdd:COG0642   251 -------------------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRG--GGTGLGLAIVKRIVELHGGTI 309
                         330
                  ....*....|....*....
gi 2425845196 489 WAESELDKGSSFHLLFPME 507
Cdd:COG0642   310 EVESEPGKGTTFTVTLPLA 328
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
134-509 1.37e-55

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 190.06  E-value: 1.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 134 ELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPCRvVLTTGEPCL-- 211
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLER-ALAEGQPVTer 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 212 DVTYVVAQGKRRlPVLSSATPLRNATGEmIGSVEILHDMSTLKALEQERE---------DFVSMLSHDLKTPITAVVGSI 282
Cdd:COG3852    80 EVTLRRKDGEER-PVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRraeklaavgELAAGLAHEIRNPLTGIRGAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 283 DLVREgRLGtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAiaeeELAPLLRRILSRFEpVALRAGIRLFL 362
Cdd:COG3852   158 QLLER-ELP--DDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPV----NLHEVLERVLELLR-AEAPKNIRIVR 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 363 HLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEPLALAGPlsaaayppanlpvAGRFLLLTVRDTGA 442
Cdd:COG3852   230 DYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQVTLGGLR-------------PRLYVRIEVIDNGP 296
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2425845196 443 GVPADCLVSIFDRFVqaknrrQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG3852   297 GIPEEILDRIFEPFF------TTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQA 357
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
90-509 2.24e-51

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: 180.54  E-value: 2.24e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  90 AVEAMKKGavDYISK-PFSSDDMKGRVERAiqYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGK 168
Cdd:COG5000    43 ATRAVAAG--DLSVRlPVTGDDEIGELARA--FNRMTDQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 169 AEELLAIRAEEVLGRPVEELLqadiPASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVlsSATPLRNatgemIGSVEILH 248
Cdd:COG5000   119 AERLLGIPLEELIGKPLEELL----PELDLAELLREALERGWQEEIELTRDGRRTLLV--RASPLRD-----DGYVIVFD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 249 DMSTLkaLEQER----EDFVSMLSHDLKTPITAVVGSIDLVRE---GRLGTINAEQKEYLDSAVESCDEMVEMIDTLLDV 321
Cdd:COG5000   188 DITEL--LRAERlaawGELARRIAHEIKNPLTPIQLSAERLRRklaDKLEEDREDLERALDTIIRQVDRLKRIVDEFLDF 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 322 HKFEAGRMQmaiaEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEI 401
Cdd:COG5000   266 ARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEV 341
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 402 RAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAknrrqgKTGGSGLGLAFCRKAM 481
Cdd:COG5000   342 STR-----------------------REDGRVRIEVSDNGPGIPEEVLERIFEPFFTT------KPKGTGLGLAIVKKIV 392
                         410       420
                  ....*....|....*....|....*...
gi 2425845196 482 DAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG5000   393 EEHGGTIELESRPGGGTTFTIRLPLAEE 420
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
5-157 8.81e-46

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: 165.14  E-value: 8.81e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG2204     4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILLTGY 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENeRLQRELDEQRQKMAAILRgMADMVVAVD 157
Cdd:COG2204    84 GDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLRREN-AEDSGLIGRSPAMQEVRR-LIEKVAPSD 154
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
5-509 3.06e-42

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 157.64  E-value: 3.06e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG4251    18 LLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVIT 164
Cdd:COG4251    98 LVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 165 LNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSATPLRNATGEMIGSV 244
Cdd:COG4251   178 LELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLEL 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 245 EILHDMST---------LKALEQEREDFVSMLSHDLKTPITAVVGSIDLVREGRLGTINAEQKEYLDSAVESCDEMVEMI 315
Cdd:COG4251   258 RLELEELEeeleertaeLERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGREYLERIRDAAERMQALI 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 316 DTLLDVHKfeAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLflHLPPAPILFpVDRSKFFRLLGNLLSNAIKFTPE 395
Cdd:COG4251   338 DDLLAYSR--VGRQELEFEPVDLNELLEEVLEDLEPRIEERGAEI--EVGPLPTVR-GDPTLLRQVFQNLISNAIKYSRP 412
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 396 E--GEIEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGktGGSGLG 473
Cdd:COG4251   413 GepPRIEIGAE-----------------------REGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEY--EGTGIG 467
                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 2425845196 474 LAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:COG4251   468 LAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
6-120 8.97e-40

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: 139.55  E-value: 8.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17550    81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIERALE 115
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
145-509 3.63e-39

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 150.50  E-value: 3.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 145 ILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRlPCRVVLTTGEPCLDVTYVVAQGKRRL 224
Cdd:PRK11360  267 ILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFAS-PLLDTLEHGTEHVDLEISFPGRDRTI 345
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 225 PVLSSATPLRNATGEMIGSVEILHDMSTLKALE-----QER----EDFVSMLSHDLKTPITAVVGSIDLVREgrlGTINA 295
Cdd:PRK11360  346 ELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQrrvarQERlaalGELVAGVAHEIRNPLTAIRGYVQIWRQ---QTSDP 422
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 296 EQKEYLDSAVESCDEMVEMIDTLLDvhkFEAGRmQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDR 375
Cdd:PRK11360  423 PSQEYLSVVLREVDRLNKVIDQLLE---FSRPR-ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWADP 498
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 376 SKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEplalagplsaaayppanlpvagRFLLLTVRDTGAGVPADCLVSIFDR 455
Cdd:PRK11360  499 ELLKQVLLNILINAVQAISARGKIRIRTWQYSD----------------------GQVAVSIEDNGCGIDPELLKKIFDP 556
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 456 FVQAKNRrqgktgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:PRK11360  557 FFTTKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQ 604
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1-120 4.90e-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: 135.36  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVV 78
Cdd:COG0784     3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALprLPDIPI 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:COG0784    83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
5-191 6.36e-38

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: 137.78  E-value: 6.36e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG0745     3 RILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTAR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQynRTRLENERLQRELDEQRQKmaailrgmadmvvaVDRQGNVIT 164
Cdd:COG0745    83 DDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLR--RRAAEVLRVGDLLDLAARE--------------VTRDGEPVE 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 2425845196 165 LNGKAEELLAI---RAEEVLGRpvEELLQA 191
Cdd:COG0745   147 LTPKEFRLLELlmrNPGRVVSR--EQLLEE 174
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
99-505 2.80e-37

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 143.19  E-value: 2.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  99 VDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAE 178
Cdd:COG5809   100 LEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIE 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 179 EVLGRPVEELLQAD--IPASRLPCRVVLTTGEPCLDVTYVVAQGKRRLpVLSSATPLrNATGEMIGSVEILHDMSTLKAL 256
Cdd:COG5809   180 ELIGKSILELIHSDdqENVAAFISQLLKDGGIAQGEVRFWTKDGRWRL-LEASGAPI-KKNGEVDGIVIIFRDITERKKL 257
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 257 EQERED---------FVSMLSHDLKTPITAVVGSIDLVRegrlGTINAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAG 327
Cdd:COG5809   258 EELLRKseklsvvgeLAAGIAHEIRNPLTSLKGFIQLLK----DTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAI 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 328 RMQmaiaEEELAPLLRRILSRFEPVALRAGIRLFLHLPP--APILFPVDRSKffRLLGNLLSNAIKFTPEEGEIEIRAEI 405
Cdd:COG5809   334 KYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDdiPDILGDENQLK--QVFINLLKNAIEAMPEGGNITIETKA 407
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 406 VAEplalagplsaaayppanlpvagRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRrqgktgGSGLGLAFCRKAMDAHD 485
Cdd:COG5809   408 EDD----------------------DKVVISVTDEGCGIPEERLKKLGEPFYTTKEK------GTGLGLMVSYKIIEEHG 459
                         410       420
                  ....*....|....*....|
gi 2425845196 486 GFVWAESELDKGSSFHLLFP 505
Cdd:COG5809   460 GKITVESEVGKGTTFSITLP 479
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
5-146 7.59e-37

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: 135.68  E-value: 7.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYP--ELVVVMMT 82
Cdd:COG3437     8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPStrDIPVIFLT 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELdeqrqKMAAIL 146
Cdd:COG3437    88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL-----KLAAPL 146
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
6-116 7.28e-36

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: 129.19  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
5-121 1.94e-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: 130.41  E-value: 1.94e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:COG3706     3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADprTADIPIIFLT 82
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQY 121
Cdd:COG3706    83 ALDDEEDRARALEAGADDYLTKPFDPEELLARVDLVARY 121
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
7-105 2.78e-35

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: 126.96  E-value: 2.78e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   7 LIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGS 86
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                          90
                  ....*....|....*....
gi 2425845196  87 EDIAVEAMKKGAVDYISKP 105
Cdd:cd00156    81 EEDAVRALELGADDYLVKP 99
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
6-135 6.07e-35

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: 127.22  E-value: 6.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADI--ALILKLQLEdiGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17549     1 VLLVDDDADVreALQQTLELA--GFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQREL 135
Cdd:cd17549    79 HGDVPMAVEAMRAGAYDFLEKPFDPERLLDVVRRALEKRRLVLENRRLRQQL 130
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
5-119 2.05e-34

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 125.29  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG5803     4 KILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTAY 83
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:COG5803    84 GELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
5-105 1.44e-33

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: 122.57  E-value: 1.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDI-GYRTVR-ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:COG4753     1 KVLIVDDEPLIREGLKRILEWEaGFEVVGeAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                          90       100
                  ....*....|....*....|...
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKP 105
Cdd:COG4753    81 GYSDFEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1-130 8.58e-33

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 121.62  E-value: 8.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDI-GYRTVR-ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVV 78
Cdd:COG4565     1 MKMIRVLIVEDDPMVAELLRRYLERLpGFEVVGvASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENER 130
Cdd:COG4565    81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
6-120 1.71e-32

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: 120.38  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17572     1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17572    81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTVRNALK 115
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
6-149 8.67e-32

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: 120.98  E-value: 8.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:COG4566     2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHG 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDE--------QRQKMAAILRGM 149
Cdd:COG4566    82 DVPMAVRAMKAGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRArlasltprEREVLDLVVAGL 153
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
7-105 9.53e-31

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: 114.81  E-value: 9.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   7 LIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGS 86
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAKDE 80
                          90
                  ....*....|....*....
gi 2425845196  87 EDIAVEAMKKGAVDYISKP 105
Cdd:cd17574    81 EEDKVLGLELGADDYITKP 99
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
5-120 1.03e-30

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: 115.19  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17569     2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLTGY 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  85 GSEDIAVEAMKKGAVD-YISKPFSSDDMKGRVERAIQ 120
Cdd:cd17569    82 ADLDAAIEAINEGEIYrFLTKPWDDEELKETIRQALE 118
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
374-507 3.47e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 110.82  E-value: 3.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVaeplalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIF 453
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD-----------------------GDHVEITVEDNGPGIPPEDLEKIF 58
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196  454 DRFVQAKNRRQgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPME 507
Cdd:smart00387  59 EPFFRTDKRSR-KIGGTGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
5-174 5.50e-29

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 119.18  E-value: 5.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK11361    6 RILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDEQRQ---------KMAAILRGMADMVVA 155
Cdd:PRK11361   86 AEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALSTSWQwghiltnspAMMDICKDTAKIALS 165
                         170       180
                  ....*....|....*....|.
gi 2425845196 156 vdrQGNVITL--NGKAEELLA 174
Cdd:PRK11361  166 ---QASVLISgeSGTGKELIA 183
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
6-120 8.13e-29

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: 110.12  E-value: 8.13e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADI--ALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:cd17536     1 VLIVDDEPLIreGLKKLIDWEELGFEVVGeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILS 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17536    81 GYDDFEYAQKAIRLGVVDYLLKPVDEEELEEALEKAKE 118
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
5-137 9.68e-29

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: 111.93  E-value: 9.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:COG4567     6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVLTGY 85
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRT---------RLENERLQRELDE 137
Cdd:COG4567    86 ASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAppenpmsldRLEWEHIQRVLAE 147
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
382-506 1.17e-28

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


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 109.50  E-value: 1.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTpEEGEIEIRAEIVAEPLALAGplsaaayppanlpvagrfLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:cd16922     5 LLNLLGNAIKFT-EEGEVTLRVSLEEEEEDGVQ------------------LRFSVEDTGIGIPEEQQARLFEPFSQADS 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2425845196 462 RRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPM 506
Cdd:cd16922    66 STTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
119-509 1.54e-28

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 116.87  E-value: 1.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 119 IQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIraeEVLGRPVEELLQAdipasrl 198
Cdd:COG3290    63 LLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEVLAE------- 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 199 pcrvVLTTGEpcLDVTYVVaqgkRRLPVLSSATPLRNaTGEMIGSVEILHDMSTLKALEQEREDFVSM------LSHDLK 272
Cdd:COG3290   133 ----VLETGE--RDEEILL----NGRVLVVNRVPIRD-DGRVVGAVATFRDRTELERLEEELEGVKELaealraQRHDFR 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 273 TPITAVVGSIDLvregrlgtinaeqKEYldsavescDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRfepv 352
Cdd:COG3290   202 NHLHTISGLLQL-------------GEY--------DEALEYIDEISEELQELIDSLLSRIGNPVLAALLLGKAAR---- 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 353 ALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAI----KFTPEEGEIEIRAEIvaeplalagplsaaayppanlpv 428
Cdd:COG3290   257 ARERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIeaveKLPEEERRVELSIRD----------------------- 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 429 AGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKnrrqgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMER 508
Cdd:COG3290   314 DGDELVIEVEDSGPGIPEELLEKIFERGFSTK-----LGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRLPKEG 388

                  .
gi 2425845196 509 S 509
Cdd:COG3290   389 E 389
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
116-506 5.28e-28

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 114.90  E-value: 5.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 116 ERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPA 195
Cdd:COG4191     2 LRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 196 SRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVLSSATPLRNATGEMIGSVEILHDMSTLKALEQeredFVSMLSHDLKTPI 275
Cdd:COG4191    82 LGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE----LAAGIAHEINNPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 276 TAVVGSIDLVREGRLGTINAEQ-KEYLDSAVESCDEMVEMIDTLLDVhkfeAGRMQMAIAEEELAPLLRRILSRFEPVAL 354
Cdd:COG4191   158 AAILGNAELLRRRLEDEPDPEElREALERILEGAERAAEIVRSLRAF----SRRDEEEREPVDLNELIDEALELLRPRLK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 355 RAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPE--EGEIEIRAEivaeplalagplsaaayppanlpVAGRF 432
Cdd:COG4191   234 ARGIEVELDLPPDLPPVLGDPGQLEQVLLNLLINAIDAMEEgeGGRITISTR-----------------------REGDY 290
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 433 LLLTVRDTGAGVPADCLVSIFDRFVQAKnrRQGKtgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPM 506
Cdd:COG4191   291 VVISVRDNGPGIPPEVLERIFEPFFTTK--PVGK--GTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
6-112 8.39e-28

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: 107.17  E-value: 8.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR---RDYPELVVVMMT 82
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIReleGGGRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMK 112
Cdd:cd17546    81 ANALEEDREKCLEAGMDDYLSKPVKLDQLK 110
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
4-119 2.21e-27

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: 106.20  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd19919     1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:cd19919    81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVERAI 116
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
5-136 5.13e-27

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 108.75  E-value: 5.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:COG3279     3 KILIVDDEPLARERLERLLEKYPDLEVvgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196  83 AHgsEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELD 136
Cdd:COG3279    83 AY--DEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
5-106 8.03e-27

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: 104.12  E-value: 8.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:cd17538     1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDpeTRHIPVIMIT 80
                          90       100
                  ....*....|....*....|....*
gi 2425845196  83 A-HGSEDIaVEAMKKGAVDYISKPF 106
Cdd:cd17538    81 AlDDREDR-IRGLEAGADDFLSKPI 104
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
5-118 2.02e-26

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: 103.45  E-value: 2.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17554     2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTAY 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  85 GS--EDIAVEAmkkgAVDYISKPFSSDDMKGRVERA 118
Cdd:cd17554    82 SEykSDFSSWA----ADAYVVKSSDLTELKETIKRL 113
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
5-105 2.13e-26

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: 103.43  E-value: 2.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17555     2 TILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGA 81
                          90       100
                  ....*....|....*....|.
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKP 105
Cdd:cd17555    82 GVMSDAVEALRLGAWDYLTKP 102
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
254-486 9.33e-26

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 109.93  E-value: 9.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 254 KALEQER---------EDFVSMLSHDLKTPITAVVGSIDLVREGRLGtinAEQKEYLDSAVESCDEMVEMIDTLLDVHKF 324
Cdd:PRK11100  241 QALESMRvklegkayvEQYVQTLTHELKSPLAAIRGAAELLQEDPPP---EDRARFTGNILTQSARLQQLIDRLLELARL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 325 EAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPIlfpvdRSKFFRL---LGNLLSNAIKFTPEEGEIEI 401
Cdd:PRK11100  318 EQRQELEVLEPVALAALLEELVEAREAQAAAKGITLRLRPDDARV-----LGDPFLLrqaLGNLLDNAIDFSPEGGTITL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 402 RAEIVAEPLAlagplsaaayppanlpvagrfllLTVRDTGAGVPADCLVSIFDRFVQAKnRRQGKTGGSGLGLAFCRKAM 481
Cdd:PRK11100  393 SAEVDGEQVA-----------------------LSVEDQGPGIPDYALPRIFERFYSLP-RPANGRKSTGLGLAFVREVA 448

                  ....*
gi 2425845196 482 DAHDG 486
Cdd:PRK11100  449 RLHGG 453
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
127-505 1.63e-25

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 109.44  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 127 ENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPCRVVLTT 206
Cdd:COG5805   144 KKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 207 G--EPCLDVTYVVAQGKRRLpVLSSATPLRNATGEMIGSVEILHDMSTLKALEQE--REDFVSML-------SHDLKTPI 275
Cdd:COG5805   224 VwqEFIIEREIITKDGRIRY-FEAVIVPLIDTDGSVKGILVILRDITEKKEAEELmaRSEKLSIAgqlaagiAHEIRNPL 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 276 TAVVGSIDLVREGRlgtinAEQKEYLDSAVESCDEMvEMIDT-LL-----DVHKFEAGRMQMAIaeEELAPLLrrilsrf 349
Cdd:COG5805   303 TSIKGFLQLLQPGI-----EDKEEYFDIMLSELDRI-ESIISeFLalakpQAVNKEKENINELI--QDVVTLL------- 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 350 EPVALRAGIRL-FLHLPPAPILFpVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpV 428
Cdd:COG5805   368 ETEAILHNIQIrLELLDEDPFIY-CDENQIKQVFINLIKNAIEAMPNGGTITIHTE-----------------------E 423
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2425845196 429 AGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRrqgktgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:COG5805   424 EDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEK------GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
7-115 2.18e-25

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: 100.43  E-value: 2.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   7 LIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMTAH 84
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDpkTSSIPIIMLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd19937    81 GEEFDKVLGLELGADDYITKPFSPRELLARV 111
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
227-505 3.20e-25

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


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 108.24  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 227 LSSATPLRNATGEMIGSVEILHDMstLKALE---QEREDFVSMLSHDLKTPITAVVG--SIDLVREgrlgTINAEQKEYL 301
Cdd:TIGR01386 207 LDQRLDPSRAPAELRELAQSFNAM--LGRLEdafQRLSQFSADLAHELRTPLTNLLGqtQVALSQP----RTGEEYREVL 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 302 DSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHlppAPILFPVDRSKFFRL 381
Cdd:TIGR01386 281 ESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVE---GEGLVRGDPQMFRRA 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:TIGR01386 358 ISNLLSNALRHTPDGGTITVRIE-----------------------RRSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDP 414
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2425845196 462 RRQGKTGGSGLGLAFCRKAMDAHDGFVWAESeLDKGSSFHLLFP 505
Cdd:TIGR01386 415 ARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
5-110 4.31e-25

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: 99.44  E-value: 4.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17563     2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTGY 81
                          90       100
                  ....*....|....*....|....*.
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDD 110
Cdd:cd17563    82 ASIATAVEAIKLGADDYLAKPADADE 107
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
374-508 6.27e-25

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: 98.98  E-value: 6.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpvAGRFLLLTVRDTGAGVPADCLVSIF 453
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAGEITVTLS------------------------EGGELTLTVEDNGIGIPPEDLPRIF 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2425845196 454 DRFVQAKNRrqgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMER 508
Cdd:pfam02518  58 EPFSTADKR---GGGGTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
PRK10490 PRK10490
sensor protein KdpD; Provisional
257-507 8.60e-25

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 108.58  E-value: 8.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 257 EQEREDFVSMLSHDLKTPITAVVG-----SIDLVREGrlgTINAEQKEYLDSAVESCDEMVemiDTLLDVHKFEAGRMQM 331
Cdd:PRK10490  661 EQLRNALLAALSHDLRTPLTVLFGqaeilTLDLASEG---SPHARQASEIRQQVLNTTRLV---NNLLDMARIQSGGFNL 734
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 332 AIAEEELAPLLRRILSRFEPVALRAGIRLflHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEpla 411
Cdd:PRK10490  735 RKEWLTLEEVVGSALQMLEPGLSGHPINL--SLPEPLTLIHVDGPLFERVLINLLENAVKYAGAQAEIGIDAHVEGE--- 809
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 412 lagplsaaayppanlpvagrFLLLTVRDTGAGVPADCLVSIFDRFvqAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAE 491
Cdd:PRK10490  810 --------------------RLQLDVWDNGPGIPPGQEQLIFDKF--ARGNKESAIPGVGLGLAICRAIVEVHGGTIWAE 867
                         250
                  ....*....|....*.
gi 2425845196 492 SELDKGSSFHLLFPME 507
Cdd:PRK10490  868 NRPEGGACFRVTLPLE 883
PRK09303 PRK09303
histidine kinase;
256-509 2.15e-24

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 104.65  E-value: 2.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 256 LEQEREDF----------VSMLSHDLKTPITAV---VGSIDLVREGRLGTINAEQKEYL-DSAVESCDEMVEMIDTLLDV 321
Cdd:PRK09303  137 LRQENETLleqlkfkdrvLAMLAHDLRTPLTAAslaLETLELGQIDEDTELKPALIEQLqDQARRQLEEIERLITDLLEV 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 322 HKFEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPP-APILFpVDRSKFFRLLGNLLSNAIKFTPEEGEIE 400
Cdd:PRK09303  217 GRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIPSdLPSVY-ADQERIRQVLLNLLDNAIKYTPEGGTIT 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 401 IRAeivaeplalagplsaaayppanLPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKnrRQGKTGGSGLGLAFCRKA 480
Cdd:PRK09303  296 LSM----------------------LHRTTQKVQVSICDTGPGIPEEEQERIFEDRVRLP--RDEGTEGYGIGLSVCRRI 351
                         250       260
                  ....*....|....*....|....*....
gi 2425845196 481 MDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:PRK09303  352 VRVHYGQIWVDSEPGQGSCFHFTLPVYRG 380
fixJ PRK09390
response regulator FixJ; Provisional
8-157 2.27e-24

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 100.46  E-value: 2.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   8 IVDDEADIALILKLQLEDIGYRtVRARDGAEA-LEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGS 86
Cdd:PRK09390    8 VVDDDEAMRDSLAFLLDSAGFE-VRLFESAQAfLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGD 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2425845196  87 EDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENE--------RLQRELDEQRQKMAAILRGMADMVVAVD 157
Cdd:PRK09390   87 VPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKSEavaadiraRIASLSERERQVMDGLVAGLSNKVIARD 165
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
5-118 2.47e-24

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: 97.73  E-value: 2.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17542     2 KVLIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERA 118
Cdd:cd17542    82 MGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKV 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
5-115 2.76e-24

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: 97.51  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRA-RDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMM 81
Cdd:cd17551     2 RILIVDDNPTNLLLLEALLRSAGYLEVVSfTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALpgLEDVPIVMI 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17551    82 TADTDREVRLRALEAGATDFLTKPFDPVELLARV 115
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
5-110 5.06e-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: 97.10  E-value: 5.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIV-DDEADIALILK-LQLEDIGYRTVRARDGAEALEILEGE-SFA------LVLLDIRMPRMDGMEVLARIRRDyPE 75
Cdd:cd17557     1 TILLVeDNPGDAELIQEaFKEAGVPNELHVVRDGEEALDFLRGEgEYAdaprpdLILLDLNMPRMDGFEVLREIKAD-PD 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2425845196  76 L----VVVMMTAHGSEDIaVEAMKKGAVDYISKPFSSDD 110
Cdd:cd17557    80 LrripVVVLTTSDAEEDI-ERAYELGANSYIVKPVDFEE 117
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
6-106 6.29e-24

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: 96.04  E-value: 6.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-----RDYPelvVVM 80
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKadpatRHIP---VIF 77
                          90       100
                  ....*....|....*....|....*.
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPF 106
Cdd:cd19920    78 LTALTDTEDKVKGFELGAVDYITKPF 103
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
6-119 1.20e-23

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: 95.74  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRtVRARDGAEA-LEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17537     3 VYVVDDDEAVRDSLAFLLRSVGLA-VKTFTSASAfLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:cd17537    82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQAL 116
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
6-116 2.98e-23

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: 94.41  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYpELVVVMMTAHG 85
Cdd:cd17614     1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTAKD 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd17614    80 SEVDKVLGLELGADDYVTKPFSNRELLARVK 110
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1-139 5.10e-23

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: 96.56  E-value: 5.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPeLVVV 79
Cdd:COG3707     1 MRGLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEERP-APVI 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI----QYNRTRLENERLQRELDEQR 139
Cdd:COG3707    80 LLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALarfrELRALRRELAKLREALEERK 143
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
4-120 6.60e-23

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: 93.77  E-value: 6.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17553     1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17553    81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYLP 117
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
5-110 3.33e-22

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: 92.07  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPeLVVVMMT 82
Cdd:cd17541     2 RVLIVDDSAVMRKLLSRILESDPDIEVvgTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAERP-TPVVMVS 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  83 AHGSE--DIAVEAMKKGAVDYISKPFSSDD 110
Cdd:cd17541    81 SLTEEgaEITLEALELGAVDFIAKPSGGIS 110
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
6-118 3.56e-22

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: 91.42  E-value: 3.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17535     1 VLIVDDHPLVREGLRRLLESEPDIEVvgEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERA 118
Cdd:cd17535    81 HDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRAV 115
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
5-118 3.96e-22

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: 91.63  E-value: 3.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMM 81
Cdd:cd19923     2 KVLVVDDFSTMRRIIKNLLKELGFNNVeEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADgaLSHLPVLMV 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERA 118
Cdd:cd19923    82 TAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKI 118
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
251-509 5.69e-22

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 98.55  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 251 STLKALEQEREDFVSMLSHDLKTPITAVVGSI----DLVREGRLGTINAEQKEyldsaVESCDEMVEmidtllDVHkfea 326
Cdd:PRK10549  231 STLEKNEQMRRDFMADISHELRTPLAVLRGELeaiqDGVRKFTPESVASLQAE-----VGTLTKLVD------DLH---- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 327 grmQMAIAEE----------ELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPvDRSKFFRLLGNLLSNAIKFTPEE 396
Cdd:PRK10549  296 ---QLSLSDEgalayrktpvDLVPLLEVAGGAFRERFASRGLTLQLSLPDSATVFG-DPDRLMQLFNNLLENSLRYTDSG 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 397 GEIEIRAEIVAEplalagplsaaayppanlpvagrFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAF 476
Cdd:PRK10549  372 GSLHISAEQRDK-----------------------TLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAI 428
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2425845196 477 CRKAMDAHDGFVWAESELDKGSSFHLLFPMERS 509
Cdd:PRK10549  429 CLNIVEAHNGRIIAAHSPFGGVSITVELPLERD 461
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
6-112 9.16e-22

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: 90.38  E-value: 9.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILE--GESFALVLLDIRMPRMDGMEVLARIRrDYPELVVVMMTA 83
Cdd:cd17584     1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRenKDEFDLVITDVHMPDMDGFEFLELIR-LEMDLPVIMMSA 79
                          90       100
                  ....*....|....*....|....*....
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMK 112
Cdd:cd17584    80 DGSTSTVMKGLAHGACDYLLKPVSIEDLK 108
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1-123 1.21e-21

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 97.41  E-value: 1.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDR--ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVV 78
Cdd:PRK10365    1 MTHDNidILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNR 123
Cdd:PRK10365   81 LIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAHTH 125
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
5-119 2.27e-21

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: 89.39  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRMP-RMDGMEVLARIRRDYPeLVVVMMT 82
Cdd:cd17534     2 KILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFLT 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:cd17534    81 AYSDEETLERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
4-116 2.65e-21

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: 89.23  E-value: 2.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMM 81
Cdd:cd17618     1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDemTRDIPIIML 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd17618    81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
6-119 3.10e-21

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: 88.70  E-value: 3.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17624     1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:cd17624    81 GVDDRVAGLDAGADDYLVKPFALEELLARL-RAL 113
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
6-105 3.17e-21

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: 88.36  E-value: 3.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd19926     1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYG 80
                          90       100
                  ....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKP 105
Cdd:cd19926    81 SLDTAIEALKAGAFDFLTKP 100
PRK15347 PRK15347
two component system sensor kinase;
267-507 3.46e-21

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 97.40  E-value: 3.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 267 LSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRIL 346
Cdd:PRK15347  405 ISHEIRTPLNGVLGALELLQNTPL---TAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTLSLEETALLPLLDQAM 481
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 347 SRFEPVALRAGIRLFLHLPP-APILFPVDRSKFFRLLGNLLSNAIKFTpEEGEIEIRAEIVAEPLAlagplsaaayppan 425
Cdd:PRK15347  482 LTIQGPAQSKSLTLRTFVGAhVPLYLHLDSLRLRQILVNLLGNAVKFT-ETGGIRLRVKRHEQQLC-------------- 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 426 lpvagrfllLTVRDTGAGVPADCLVSIFDRFVQAknrrQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:PRK15347  547 ---------FTVEDTGCGIDIQQQQQIFTPFYQA----DTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLP 613

                  ..
gi 2425845196 506 ME 507
Cdd:PRK15347  614 LN 615
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
1-123 4.08e-21

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 96.09  E-value: 4.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVM 80
Cdd:PRK10923    1 MQRGIVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVII 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNR 123
Cdd:PRK10923   81 MTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAISHYQ 123
orf27 CHL00148
Ycf27; Reviewed
5-115 8.21e-21

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 91.32  E-value: 8.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRR--DYPelvVVMMT 82
Cdd:CHL00148    8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKesDVP---IIMLT 84
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:CHL00148   85 ALGDVSDRITGLELGADDYVVKPFSPKELEARI 117
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
6-105 9.53e-21

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: 87.11  E-value: 9.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLMLTARD 80
                          90       100
                  ....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKP 105
Cdd:cd19935    81 SVEDRVKGLDLGADDYLVKP 100
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
5-117 1.09e-20

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: 87.21  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:cd17548     1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDpaTRDIPVIALT 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVER 117
Cdd:cd17548    81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
123-505 1.46e-20

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 93.92  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 123 RTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL----------QAD 192
Cdd:PRK11006   81 QMQLRNRKRRRELGNLIKRFRSGAESLPDAVVLTTEEGNIFWCNGLAQQLLGFRWPEDNGQNILNLLrypeftqylkTRD 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 193 IpaSRlPCRVVLTTGEpCLDVtyvvaqgkRRLPVlssatplrnATGEMIgsvEILHDMSTLKALEQEREDFVSMLSHDLK 272
Cdd:PRK11006  161 F--SR-PLTLVLNNGR-HLEI--------RVMPY---------TEGQLL---MVARDVTQMHQLEGARRNFFANVSHELR 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 273 TPITAVVGSIDL---------VREGRLGTINaEQKEYLDSAVEScdemvemidtLLDVHKFEAGRMqMAIAEEELAPLLR 343
Cdd:PRK11006  217 TPLTVLQGYLEMmqdqplegaLREKALHTMR-EQTQRMEGLVKQ----------LLTLSKIEAAPT-IDLNEKVDVPMML 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 344 RILSRfEPVALRAGirlfLHlppaPILFPVDRSkfFRLLG----------NLLSNAIKFTPEEGEIEIRAEIVAeplalA 413
Cdd:PRK11006  285 RVLER-EAQTLSQG----KH----TITFEVDNS--LKVFGnedqlrsaisNLVYNAVNHTPEGTHITVRWQRVP-----Q 348
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 414 GPLsaaayppanlpvagrfllLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESE 493
Cdd:PRK11006  349 GAE------------------FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESE 410
                         410
                  ....*....|..
gi 2425845196 494 LDKGSSFHLLFP 505
Cdd:PRK11006  411 VGKGTRFSFVLP 422
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
7-116 1.93e-20

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: 86.51  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   7 LIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGS 86
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  87 EDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd17625    81 VEDRVKGLDLGADDYLPKPFSLAELLARIR 110
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
5-132 2.53e-20

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 89.70  E-value: 2.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:TIGR02154   4 RILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRpeTRAIPIIMLT 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQ 132
Cdd:TIGR02154  84 ARGEEEDRVRGLETGADDYITKPFSPRELLARIKAVLRRIRPQLSDEVIE 133
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
6-110 5.29e-20

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 85.20  E-value: 5.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYP--ELVVVMMTA 83
Cdd:cd17580     1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWlaNTPAIALTG 80
                          90       100
                  ....*....|....*....|....*..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDD 110
Cdd:cd17580    81 YGQPEDRERALEAGFDAHLVKPVDPDE 107
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
5-111 7.07e-20

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: 85.04  E-value: 7.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-----RDYPelvVV 79
Cdd:cd17562     2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRklpayKFTP---IL 78
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:cd17562    79 MLTTESSDEKKQEGKAAGATGWLVKPFDPEQL 110
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
6-115 1.17e-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: 84.36  E-value: 1.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTARD 80
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17627    81 SVSDRVAGLDAGADDYLVKPFALEELLARV 110
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
5-119 1.58e-19

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: 83.94  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:cd17615     1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAK 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:cd17615    81 DSVEDRIAGLTAGGDDYVTKPFSLEEVVARL-RAL 114
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
6-116 2.06e-19

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: 83.87  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd19934    81 SWQDKVEGLDAGADDYLTKPFHIEELLARLR 111
PRK15115 PRK15115
response regulator GlrR; Provisional
5-174 2.45e-19

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 90.28  E-value: 2.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK15115    7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAH 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYnRTRLENERLQRELDEQRQKMAAILRgMADMVVAVDRQGNVIT 164
Cdd:PRK15115   87 GSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQ-SAPATDERWREAIVTRSPLMLRLLE-QARMVAQSDVSVLING 164
                         170
                  ....*....|
gi 2425845196 165 LNGKAEELLA 174
Cdd:PRK15115  165 QSGTGKEILA 174
PRK15479 PRK15479
transcriptional regulator TctD;
5-119 2.84e-19

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 86.70  E-value: 2.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTAR 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:PRK15479   82 SAVADRVKGLNVGADDYLPKPFELEELDARL-RAL 115
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
5-115 4.15e-19

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: 82.95  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGES-FALVLLDIRMPRMDGMEVLARIRRDYP--ELVVVMM 81
Cdd:cd17544     2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGI 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17544    82 SASGDNALSARFIKAGANDFLTKPFLPEEFYCRV 115
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
242-507 4.81e-19

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 90.95  E-value: 4.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  242 GSVEILHDMSTLKALEQER----------EDFVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQK-EYLDSAVESCDE 310
Cdd:PRK09959   684 GWQDITETRDLIHALEVERnkainatvakSQFLATMSHEIRTPISSIMGFLELLSGSGL---SKEQRvEAISLAYATGQS 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  311 MVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLP-PAPILFPVDRSKFFRLLGNLLSNA 389
Cdd:PRK09959   761 LLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTfPDHYLVKIDPQAFKQVLSNLLSNA 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  390 IKFTpEEGEIEIRAEIVaeplalagplsaaayppaNLPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQgkTGG 469
Cdd:PRK09959   841 LKFT-TEGAVKITTSLG------------------HIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQ--QTG 899
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 2425845196  470 SGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPME 507
Cdd:PRK09959   900 SGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVE 937
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
257-509 5.04e-19

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 90.73  E-value: 5.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 257 EQEREDFVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEE 336
Cdd:PRK11466  441 SQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPA---LNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNVSVSDE 517
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 337 ELAP------LLRRILSRFEPVALRAGIRLFLHLPPApilFPVDRSKFFRLLGNLLSNAIKFTpEEGEIEIRAEivaepl 410
Cdd:PRK11466  518 PFEPrpllesTLQLMSGRVKGRPIRLATDIADDLPTA---LMGDPRRIRQVITNLLSNALRFT-DEGSIVLRSR------ 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 411 alagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRqgktGGSGLGLAFCRKAMDAHDGFVWA 490
Cdd:PRK11466  588 -----------------TDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKR----GGTGLGLTISSRLAQAMGGELSA 646
                         250
                  ....*....|....*....
gi 2425845196 491 ESELDKGSSFHLLFPMERS 509
Cdd:PRK11466  647 TSTPEVGSCFCLRLPLRVA 665
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
1-119 5.85e-19

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 86.01  E-value: 5.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNgdRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEgESFALVLLDIRMPRMDGMEVLARIRRDYpELVVVM 80
Cdd:PRK10955    1 MN--KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQTH-QTPVIM 76
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:PRK10955   77 LTARGSELDRVLGLELGADDYLPKPFNDRELVARI-RAI 114
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
4-135 1.18e-18

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: 82.03  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDiGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17596     1 PTILVVDDEVRSLEALRRTLEE-DFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2425845196  84 HG-SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQREL 135
Cdd:cd17596    80 YTdSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
232-502 1.39e-18

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 89.23  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 232 PLRNATGEMIGSVEILHDMSTLK----ALE---QEREDFVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSA 304
Cdd:PRK11091  248 PFYDRVGKRHGLMGFGRDITERKryqdALEkasRDKTTFISTISHELRTPLNGIVGLSRILLDTEL---TAEQRKYLKTI 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 305 VESCDEMVEMIDTLLDVHKFEAGRMQMA---------IAE-EELAPLLrrilsrfepvALRAGIRLFLH-LPPAPILFPV 373
Cdd:PRK11091  325 HVSAITLGNIFNDIIDMDKMERRKLQLDnqpidftdfLADlENLSGLQ----------AEQKGLRFDLEpLLPLPHKVIT 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTpEEGEIEIRaeIVAEPlalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIF 453
Cdd:PRK11091  395 DGTRLRQILWNLISNAVKFT-QQGGVTVR--VRYEE--------------------GDMLTFEVEDSGIGIPEDELDKIF 451
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196 454 DRFVQAKNRRQGKTG-GSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHL 502
Cdd:PRK11091  452 AMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTL 501
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
5-119 1.59e-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: 81.31  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVlARIRRDYPELVVVMMTA 83
Cdd:cd19932     2 RVLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEA-AKIITSENIAPIVLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:cd19932    81 YSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAI 116
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
245-506 1.61e-18

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 89.26  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 245 EILHDMSTlkALEQERED---FVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSAVESCDEMVEMIDTLLDV 321
Cdd:PRK10841  431 ESLQEMAQ--AAEQASQSksmFLATVSHELRTPLYGIIGNLDLLQTKEL---PKGVDRLVTAMNNSSSLLLKIISDILDF 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 322 HKFEAgrMQMAIAEEELAP--LLRRILSRFEPVALRAGIRLFLHLPP-APILFPVDRSKFFRLLGNLLSNAIKFTpEEGE 398
Cdd:PRK10841  506 SKIES--EQLKIEPREFSPreVINHITANYLPLVVKKRLGLYCFIEPdVPVALNGDPMRLQQVISNLLSNAIKFT-DTGC 582
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 399 IEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCR 478
Cdd:PRK10841  583 IVLHVR-----------------------VDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICE 639
                         250       260
                  ....*....|....*....|....*...
gi 2425845196 479 KAMDAHDGFVWAESELDKGSSFHLLFPM 506
Cdd:PRK10841  640 KLINMMDGDISVDSEPGMGSQFTIRIPL 667
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
374-505 2.76e-18

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


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 80.20  E-value: 2.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAeivaeplalagplsaaayppANLPVAGRfllLTVRDTGAGVPADCLVSIF 453
Cdd:cd16946     1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRA--------------------AQTPQEVR---LDVEDSAPGVSDDQLARLF 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196 454 DRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16946    58 ERFYRVESSRNRASGGSGLGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1-119 3.32e-18

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 83.47  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIA--LILKLQLEdiGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVV 78
Cdd:PRK11083    1 MQQPTILLVEDEQAIAdtLVYALQSE--GFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPV 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:PRK11083   79 IFLTARSDEVDRLVGLEIGADDYVAKPFSPREVAARV-RTI 118
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
6-105 4.66e-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: 79.34  E-value: 4.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRR--DYPELVVVMMTA 83
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKnaDFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd19927    81 KGMTSDRIKGYNAGCDGYLSKP 102
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
5-120 5.94e-18

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: 79.90  E-value: 5.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDI-GYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPE---LVVVM 80
Cdd:cd17552     3 RILVIDDEEDIREVVQACLEKLaGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQAN-PEtqsIPVIL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17552    82 LTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAKLLG 121
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
6-118 6.85e-18

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: 79.50  E-value: 6.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17532     1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  84 HgsEDIAVEAMKKGAVDYISKPFSSDDMKGRVERA 118
Cdd:cd17532    81 Y--DEYAVEAFELNAVDYLLKPFSEERLAEALAKL 113
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
132-281 8.12e-18

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 85.59  E-value: 8.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 132 QRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELlqadIPASRLpcRVVLTTGEPCL 211
Cdd:COG3829     3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL----IPNSPL--LEVLKTGKPVT 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 212 DVTYVVaqGKRRLPVLSSATPLRNAtGEMIGSVEILHDMSTLKALEQEREDFVSMLSHDLKTPITAVVGS 281
Cdd:COG3829    77 GVIQKT--GGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDIIGK 143
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
6-120 1.37e-17

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: 78.50  E-value: 1.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPELVVVMMTAHG 85
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTARG 79
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAIQ 120
Cdd:cd17623    80 DDIDRILGLELGADDYLPKPFNPRELVARI-RAIL 113
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
5-117 2.35e-17

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: 78.06  E-value: 2.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:cd19925     2 NVLIVEDDPMVAEIHRAYVEQVPGFTVigTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVVT 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVER 117
Cdd:cd19925    82 AANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
6-105 3.33e-17

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


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 76.82  E-value: 3.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIrRDYPELVVVMMTAHG 85
Cdd:cd17620     1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRL-REWSAVPVIVLSARD 79
                          90       100
                  ....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKP 105
Cdd:cd17620    80 EESDKIAALDAGADDYLTKP 99
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
6-105 1.00e-16

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: 75.56  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPELVVVMMTAHG 85
Cdd:cd19936     1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK-STLPVIFLTSKD 79
                          90       100
                  ....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKP 105
Cdd:cd19936    80 DEIDEVFGLRMGADDYITKP 99
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
5-106 2.48e-16

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: 74.57  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILK---LQLEDIGYRTVrARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR--RDYPELVVV 79
Cdd:cd17561     3 KVLIADDNREFVQLLEeylNSQPDMEVVGV-AHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRrmRLEKRPKII 81
                          90       100
                  ....*....|....*....|....*..
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPF 106
Cdd:cd17561    82 MLTAFGQEDITQRAVELGASYYILKPF 108
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
5-106 2.64e-16

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: 74.46  E-value: 2.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILE-GESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd18160     1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQqGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                          90       100
                  ....*....|....*....|...
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPF 106
Cdd:cd18160    81 GAAAAPELLSDAVGDNATLKKPF 103
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
375-508 2.68e-16

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 74.55  E-value: 2.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 375 RSKFfrllGNLLSNAIKFTPEEGEIEIRAEivAEPlalagplSAAAyppanlpvagrfllLTVRDTGAGVPADCLVSIFD 454
Cdd:cd16952     2 RSAF----SNLVSNAVKYTPPSDTITVRWS--QEE-------SGAR--------------LSVEDTGPGIPPEHIPRLTE 54
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 455 RFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMER 508
Cdd:cd16952    55 RFYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFPSSR 108
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
240-505 1.37e-15

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 79.05  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 240 MIGSVEilhDMSTLKAleqereDFVSMLSHDLKTPITAVVGSIDLV-REGRlgtINAEQKEYLDSAVESCDEMVEMIDTL 318
Cdd:PRK09835  251 MIERIE---DVFTRQS------NFSADIAHEIRTPITNLITQTEIAlSQSR---SQKELEDVLYSNLEELTRMAKMVSDM 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 319 LDVHKFEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLflHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGE 398
Cdd:PRK09835  319 LFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVEL--RFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 399 IEIRAEIVAEplalagplsaaayppanlpvagrFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLGLAFCR 478
Cdd:PRK09835  397 ITVRCQEVDH-----------------------QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVK 453
                         250       260
                  ....*....|....*....|....*..
gi 2425845196 479 KAMDAHDGFVWAESELDkGSSFHLLFP 505
Cdd:PRK09835  454 SIVVAHKGTVAVTSDAR-GTRFVISLP 479
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
5-110 1.49e-15

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: 72.57  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEAdIA--LILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-RDYPELVVVMm 81
Cdd:cd17593     2 KVLICDDSS-MArkQLARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPvEQLETKVIVV- 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196  82 tahgSEDIAVEAMKK----GAVDYISKPFSSDD 110
Cdd:cd17593    80 ----SGDVQPEAKERvlelGALAFLKKPFDPEK 108
PRK10610 PRK10610
chemotaxis protein CheY;
5-117 1.77e-15

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 73.08  E-value: 1.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMM 81
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGFNNVEeAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADgaMSALPVLMV 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVER 117
Cdd:PRK10610   87 TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNK 122
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
5-116 1.78e-15

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: 72.41  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRdYPELVVVMMTAH 84
Cdd:cd19938     1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR-FSDVPIIMVTAR 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd19938    80 VEEIDRLLGLELGADDYICKPYSPREVVARVK 111
PRK13557 PRK13557
histidine kinase; Provisional
4-119 2.23e-15

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 78.56  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGES-FALVLLDIRMP-RMDGMeVLAR-IRRDYPELVVVM 80
Cdd:PRK13557  416 ETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPeVDLLFTDLIMPgGMNGV-MLAReARRRQPKIKVLL 494
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:PRK13557  495 TTGYAEASIERTDAGGSEFDILNKPYRRAELARRVRMVL 533
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
374-505 2.52e-15

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 71.75  E-value: 2.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEPLALagplsaaayppanlpvagrfllLTVRDTGAGVPADCLVSIF 453
Cdd:cd16925     1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRLNRFL----------------------LTVSDSGPGIPPNLREEIF 58
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196 454 DRFVQAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16925    59 ERFRQGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
5-126 2.92e-15

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: 71.73  E-value: 2.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPELVVVMMTAH 84
Cdd:cd17626     2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE-SGVPIVMLTAK 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeraiqynRTRL 126
Cdd:cd17626    81 SDTVDVVLGLESGADDYVAKPFKPKELVARI-------RARL 115
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
381-505 2.98e-15

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 71.59  E-value: 2.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 381 LLGNLLSNAIKFTPEE--GEIEIRAEIVAEPLALAgplsaaayppanlpvagrfllltVRDTGAGVP---ADCLVSIFDR 455
Cdd:cd16921     4 VLTNLLGNAIKFRRPRrpPRIEVGAEDVGEEWTFY-----------------------VRDNGIGIDpeyAEKVFGIFQR 60
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196 456 FvqaknRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16921    61 L-----HSREEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
378-506 4.63e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 70.82  E-value: 4.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 378 FFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIFDRFV 457
Cdd:cd16949     1 LARALENVLRNALRYSPSKILLDISQD-------------------------GDQWTITITDDGPGVPEDQLEQIFLPFY 55
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2425845196 458 QAKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPM 506
Cdd:cd16949    56 RVDSARDRESGGTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
6-106 7.68e-15

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: 70.45  E-value: 7.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILE-GESFALVLLDIRMPR-MDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd18161     1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLEsGPDIDLLVTDVIMPGgMNGSQLAEEARRRRPDLKVLLTSG 80
                          90       100
                  ....*....|....*....|...
gi 2425845196  84 HGSEDIAVEAMKKGaVDYISKPF 106
Cdd:cd18161    81 YAENAIEGGDLAPG-VDVLSKPF 102
ompR PRK09468
osmolarity response regulator; Provisional
2-115 9.30e-15

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 73.85  E-value: 9.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   2 NGDRILIVDDEADIALILKLQLEDIGYRtVRARDGAEALE-ILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVM 80
Cdd:PRK09468    4 ENYKILVVDDDMRLRALLERYLTEQGFQ-VRSAANAEQMDrLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPTPIIM 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:PRK09468   83 LTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARI 117
PRK15347 PRK15347
two component system sensor kinase;
5-181 9.51e-15

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 77.37  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDeADIAL-ILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDY----PELVVV 79
Cdd:PRK15347  692 QILLVDD-VETNRdIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnldPDCMIV 770
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYnrtrleneRLQR--ELDEQRQKMAAILrGMADMVVAVD 157
Cdd:PRK15347  771 ALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALELAAEY--------QLLRgiELSPQDSSCSPLL-DTDDMALNSK 841
                         170       180
                  ....*....|....*....|....
gi 2425845196 158 RQGNVITLNGKAEEllAIRAEEVL 181
Cdd:PRK15347  842 LYQSLLLLLAQIEQ--AVENQEVL 863
spore_0_A TIGR02875
sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a ...
5-115 1.13e-14

sporulation transcription factor Spo0A; Spo0A, the stage 0 sporulation protein A, is a transcription factor critical for the initiation of sporulation. It contains a response regulator receiver domain (pfam00072). In Bacillus subtilis, it works together with response regulator Spo0F and the phosphotransferase Spo0B, both of which are missing from at least some sporulating species and thus not part of the endospore forming bacteria minimal gene set. Spo0A, however, is universal among endospore-forming species. [Cellular processes, Sporulation and germination]


Pssm-ID: 131922 [Multi-domain]  Cd Length: 262  Bit Score: 74.06  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQL---EDIGYRTVrARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRR--DYPELVVV 79
Cdd:TIGR02875   4 RIVIADDNKEFCNLLKEYLaaqPDMEVVGV-AHNGVDALELIKEQQPDVVVLDIIMPHLDGIGVLEKLNEieLSARPRVI 82
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:TIGR02875  83 MLSAFGQEKITQRAVALGADYYVLKPFDLEILAARI 118
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
6-117 1.26e-14

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: 70.05  E-value: 1.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPEL----VVVMM 81
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSD-PDLkdipVILLT 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  82 TAHGSEDIaVEAMKKGAVDYISKPFSSDDMKGRVER 117
Cdd:cd17598    80 TLSDPRDV-IRGLECGADNFITKPYDEKYLLSRIKY 114
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
2-137 1.74e-14

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 73.18  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   2 NGDRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRdYPELVVVMM 81
Cdd:PRK10710    9 NTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR-FSDIPIVMV 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeraiqynRTRLENERLQRELDE 137
Cdd:PRK10710   88 TAKIEEIDRLLGLEIGADDYICKPYSPREVVARV-------KTILRRCKPQRELQQ 136
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
6-119 1.82e-14

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: 69.62  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd18159     1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISNVPIIFISSRDD 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196  86 SEDIaVEAMKKGAVDYISKPFSSDDMKGRVERAI 119
Cdd:cd18159    81 NMDQ-VMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
4-115 2.09e-14

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: 69.34  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMeVLARIRRDYPELVVVMMTA 83
Cdd:cd17619     1 PHILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGL-SLTRELREQSEVGIILVTG 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17619    80 RDDEVDRIVGLEIGADDYVTKPFNPRELLVRA 111
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-108 4.19e-14

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 73.65  E-value: 4.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKL------QLEDIGyrtvRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPeLVV 78
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEilnsdpDIEVVG----TAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLRP-TPV 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196  79 VM---MTAHGSEdIAVEAMKKGAVDYISKPFSS 108
Cdd:PRK00742   80 VMvssLTERGAE-ITLRALELGAVDFVTKPFLG 111
PRK10643 PRK10643
two-component system response regulator PmrA;
5-193 4.70e-14

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 71.22  E-value: 4.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYTLPVLILTAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENErLQRE---LDEQRQKmaailrgmadmvvaVDRQGN 161
Cdd:PRK10643   82 DTLEDRVAGLDVGADDYLVKPFALEELHARIRALIRRHQGQGENE-LQVGnltLNLGRQQ--------------VWLDGQ 146
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2425845196 162 VITLNGKAEELLA---IRAeevlGRPVE-ELLQADI 193
Cdd:PRK10643  147 ELILTPKEFALLSrlmLKA----GSPVHrEILYQDI 178
pleD PRK09581
response regulator PleD; Reviewed
5-105 5.17e-14

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 74.17  E-value: 5.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDD-EADIALI-LKLQLEdigYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDY-----Pel 76
Cdd:PRK09581    4 RILVVDDiPANVKLLeAKLLAE---YYTVlTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPatthiP-- 78
                          90       100
                  ....*....|....*....|....*....
gi 2425845196  77 vVVMMTAHGSEDIAVEAMKKGAVDYISKP 105
Cdd:PRK09581   79 -VVMVTALDDPEDRVRGLEAGADDFLTKP 106
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
299-505 5.71e-14

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 74.71  E-value: 5.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 299 EYLDSAVESCDEMVEMIDTLLDVHKFEAGRMQMAIAEE---ELAPLLRrilsrfepVALRAGIRLFLHLPPAPILFPVDR 375
Cdd:PRK13837  487 RYIDEIISAGARARLIIDQILAFGRKGERNTKPFDLSElvtEIAPLLR--------VSLPPGVELDFDQDQEPAVVEGNP 558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 376 SKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEPLALAgpLSAAAYPPanlpvaGRFLLLTVRDTGAGVPADCLVSIFDR 455
Cdd:PRK13837  559 AELQQVLMNLCSNAAQAMDGAGRVDISLSRAKLRAPKV--LSHGVLPP------GRYVLLRVSDTGAGIDEAVLPHIFEP 630
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196 456 FVQAKNrrqgktGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:PRK13837  631 FFTTRA------GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDVYLP 674
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
241-507 6.66e-14

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 74.50  E-value: 6.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 241 IGSVEIlhDMSTLKALEQER--EDFVSMLSHDLKTPITAVVGSIDLVregrLGT-INAEQKEYLDSAVESCDEMVEMIDT 317
Cdd:PRK11107  274 IQNVEL--DLAKKRAQEAARikSEFLANMSHELRTPLNGVIGFTRQT----LKTpLTPTQRDYLQTIERSANNLLAIIND 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 318 LLDVHKFEAGRMQMaiaeEELAPLLRRILSrfEPVALRA------GIRLFLHLPP-APILFPVDRSKFFRLLGNLLSNAI 390
Cdd:PRK11107  348 ILDFSKLEAGKLVL----ENIPFSLRETLD--EVVTLLAhsahekGLELTLNIDPdVPDNVIGDPLRLQQIITNLVGNAI 421
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 391 KFTpEEGEIEIRAEIVAEplalagplsaaayppANLPVAGRFLlltVRDTGAGVPADCLVSIFDRFVQAK---NRRQGkt 467
Cdd:PRK11107  422 KFT-ESGNIDILVELRAL---------------SNTKVQLEVQ---IRDTGIGISERQQSQLFQAFRQADasiSRRHG-- 480
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2425845196 468 gGSGLGLAFCRK---AMDAHDGFvwaESELDKGSSFHLLFPME 507
Cdd:PRK11107  481 -GTGLGLVITQKlvnEMGGDISF---HSQPNRGSTFWFHLPLD 519
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
5-116 8.56e-14

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: 67.78  E-value: 8.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYpELVVVMMTAH 84
Cdd:cd19939     1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTAR 79
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:cd19939    80 TEEMDRVLGLEMGADDYLCKPFSPRELLARVR 111
envZ PRK09467
osmolarity sensor protein; Provisional
250-488 9.73e-14

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 73.02  E-value: 9.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 250 MST-LKALEQEREDFVSMLSHDLKTPITAVvgsidlvregRLGT-INAEQKEYL-DSAVESCDEMVEMIDTLLDVHKFEA 326
Cdd:PRK09467  218 MAAgIKQLEDDRTLLMAGVSHDLRTPLTRI----------RLATeMMSEEDGYLaESINKDIEECNAIIEQFIDYLRTGQ 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 327 grmQMAIAEEELAPLLRrilsrfEPVALRAGIR--LFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTpeEGEIEIRAE 404
Cdd:PRK09467  288 ---EMPMEMADLNALLG------EVIAAESGYEreIETALQPGPIEVPMNPIAIKRALANLVVNAARYG--NGWIKVSSG 356
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 405 ivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRqgKTGGSGLGLAFCRKAMDAH 484
Cdd:PRK09467  357 -----------------------TEGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSAR--GSSGTGLGLAIVKRIVDQH 411

                  ....
gi 2425845196 485 DGFV 488
Cdd:PRK09467  412 NGKV 415
PRK11517 PRK11517
DNA-binding response regulator HprR;
5-185 2.21e-13

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 69.54  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLaRIRRDYPELVVVMMTAH 84
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQIL-QTLRTAKQTPVICLTAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAiQYNRTRLENERLQ---RELDEQRQkmaailrgmadmvvAVDRQGN 161
Cdd:PRK11517   81 DSVDDRVRGLDSGANDYLVKPFSFSELLARV-RA-QLRQHHALNSTLEisgLRMDSVSQ--------------SVSRDNI 144
                         170       180
                  ....*....|....*....|....*..
gi 2425845196 162 VITLNGKAEE---LLAIRAEEVLGRPV 185
Cdd:PRK11517  145 SITLTRKEFQllwLLASRAGEIIPRTV 171
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
5-120 2.39e-13

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 69.36  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD--YPELVVVMMT 82
Cdd:PRK10161    4 RILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKREsmTRDIPVVMLT 83
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:PRK10161   84 ARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMR 121
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
5-58 2.50e-13

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: 64.51  E-value: 2.50e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2425845196    5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMP 58
Cdd:smart00448   2 RILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
6-105 2.63e-13

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: 66.98  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEAD----IALILKLQLEDiGYRTVRARDGAEALEILE-----GESFALVLLDIRMPRMDGMEVLARIRRDYPEL 76
Cdd:cd17595     3 ILTVDDDPQvlraVARDLRRQYGK-DYRVLRADSGAEALDALKelklrGEAVALFLVDQRMPEMDGVEFLEKAMELFPEA 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  77 VVVMMTAHGSEDIAVEAMKKGAVD-YISKP 105
Cdd:cd17595    82 KRVLLTAYADTDAAIRAINDVQLDyYLLKP 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
130-259 3.41e-13

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 69.67  E-value: 3.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 130 RLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPC-RVVLTTGE 208
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELlRAALAGGG 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2425845196 209 PCLDVTYVVAQGKRRLPVLSSATPLRNATGEMIGSVEILHDMSTLKALEQE 259
Cdd:COG2202    81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEA 131
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
6-105 4.52e-13

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: 65.11  E-value: 4.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVD-DEADIALILKLqLEDIGYRTVRARDGAEALEILEGESFA--LVLLDIRMPRMDGMEVLARI-----RRDYPelv 77
Cdd:cd17582     1 VLLVEnDDSTRQIVTAL-LRKCSYEVTAASDGLQAWDVLEDEQNEidLILTEVDLPVSSGFKLLSYImrhkiCKNIP--- 76
                          90       100
                  ....*....|....*....|....*...
gi 2425845196  78 VVMMTAHGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd17582    77 VIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
4-108 4.85e-13

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: 65.48  E-value: 4.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   4 DRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYpELVVVMMTA 83
Cdd:cd17622     1 TRILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKY-QGPILLLTA 79
                          90       100
                  ....*....|....*....|....*
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSS 108
Cdd:cd17622    80 LDSDIDHILGLELGADDYVVKPVEP 104
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
259-327 7.03e-13

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 63.38  E-value: 7.03e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2425845196 259 EREDFVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAG 327
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKL---DEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
140-250 7.84e-13

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 64.75  E-value: 7.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 140 QKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPC-RVVLTTGEPCL--DVTYV 216
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELlRQALLQGEESRgfEVSFR 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196 217 VAQGKRRlPVLSSATPLRNATGEMIGSVEILHDM 250
Cdd:pfam00989  81 VPDGRPR-HVEVRASPVRDAGGEILGFLGVLRDI 113
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
6-105 1.19e-12

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: 64.32  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEG---------ESFALVLLDIRMPRMDGMEVLARIRRD--YP 74
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENlakegndlsKELDLIITDIEMPKMDGYELTFELRDDprLA 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  75 ELVVVMMTAHGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd19924    81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
6-115 1.19e-12

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: 64.37  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTvrarDGAEALEilEGE------SFALVLLDIRMPRMDGMEVLARIRRDYPELVVV 79
Cdd:cd17573     1 ILLIEDDSTLGKEISKGLNEKGYQA----DVAESLK--DGEyyidirNYDLVLVSDKLPDGNGLSIVSRIKEKHPSIVVI 74
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17573    75 VLSDNPKTEQEIEAFKEGADDYIAKPFDFKVLVARI 110
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
259-327 2.04e-12

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 62.20  E-value: 2.04e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2425845196  259 EREDFVSMLSHDLKTPITAVVGSIDLVREGRLgtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHKFEAG 327
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTEL---SEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
257-323 4.69e-12

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 61.07  E-value: 4.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2425845196 257 EQEREDFVSMLSHDLKTPITAVVGSIDLVREGRLGtiNAEQKEYLDSAVESCDEMVEMIDTLLDVHK 323
Cdd:cd00082     1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLD--DEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
6-115 5.01e-12

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: 62.46  E-value: 5.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPELVVVMMTAHG 85
Cdd:cd17594     2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR-SDVPIIIISGDR 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  86 SEDIA-VEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17594    81 RDEIDrVVGLELGADDYLAKPFGLRELLARV 111
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
6-105 6.96e-12

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: 61.75  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRtVRARDGAEALE--ILEGESfALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYE-VRTTGNAATLWrwVEEGEG-DLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSA 78
                          90       100
                  ....*....|....*....|..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd19928    79 QNTLMTAVKAAERGAFEYLPKP 100
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
384-505 7.80e-12

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 62.01  E-value: 7.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 384 NLLSNAIKFTPEEGEIEIRAEIvaEPLALAGPLSAAAYPPanlpvaGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNrr 463
Cdd:cd16919     7 NLAVNARDAMPEGGRLTIETSN--QRVDADYALNYRDLIP------GNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKE-- 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2425845196 464 QGKtgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16919    77 VGK--GTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
382-505 8.64e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 61.92  E-value: 8.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTPEEGEIEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:cd16948    10 IGQIVSNALKYSKQGGKIEIYSE-----------------------TNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGEN 66
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2425845196 462 RRQGKTgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16948    67 GRNFQE-STGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
340-504 1.37e-11

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 61.88  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 340 PLLRRILSRFEPVALRAGIRLFLHLPPApILFPVDRSKFFRLLGNLLSNAIKFTPEEGEieiraeivaeplalagpLSAA 419
Cdd:cd16954     1 PLLDSLCSALNKVYQRKGVSISLDISPE-LRFPGERNDLMELLGNLLDNACKWCLEFVE-----------------VTAR 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 420 AYPPAnlpvagrfLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKtggsGLGLAFCRKAMDAHDGFVWAESELDKGSS 499
Cdd:cd16954    63 QTDGG--------LHLIVDDDGPGVPESQRSKIFQRGQRLDEQRPGQ----GLGLAIAKEIVEQYGGELSLSDSPLGGAR 130

                  ....*
gi 2425845196 500 FHLLF 504
Cdd:cd16954   131 FEVVF 135
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
6-115 1.90e-11

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: 61.12  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRM-PRMDGMEVLARIRRDY---PELVVVM 80
Cdd:cd17589     1 FLIVDDQPTFRSMLKSMLRSLGVTRIDtASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELRHKKlisPSTVFIM 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRV 115
Cdd:cd17589    81 VTGESSRAMVLSALELEPDDYLLKPFTVSELRERL 115
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
6-111 3.96e-11

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: 59.98  E-value: 3.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADI--ALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd19930     1 VLIAEDQEMVrgALAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                          90       100
                  ....*....|....*....|....*...
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:cd19930    81 FGRPGYFRRALAAGVDGYVLKDRPIEEL 108
PRK11173 PRK11173
two-component response regulator; Provisional
1-129 4.31e-11

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 63.11  E-value: 4.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMeVLARIRRDYPELVVVM 80
Cdd:PRK11173    1 MQTPHILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGL-LLARELREQANVALMF 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQynRTRLENE 129
Cdd:PRK11173   80 LTGRDNEVDKILGLEIGADDYITKPFNPRELTIRARNLLS--RTMNLGT 126
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
5-105 4.64e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 64.13  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLE-DIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARI--RRDYPELVVVM 80
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALArDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRImaERPCPILIVTS 81
                          90       100
                  ....*....|....*....|....*
gi 2425845196  81 MTAHGSEDIaVEAMKKGAVDYISKP 105
Cdd:PRK12555   82 LTERNASRV-FEAMGAGALDAVDTP 105
PRK10766 PRK10766
two-component system response regulator TorR;
5-106 5.24e-11

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 62.36  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMeVLARIRRDYPELVVVMMTAH 84
Cdd:PRK10766    4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGL-MLTRELRSRSTVGIILVTGR 82
                          90       100
                  ....*....|....*....|..
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPF 106
Cdd:PRK10766   83 TDSIDRIVGLEMGADDYVTKPL 104
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
2-112 5.94e-11

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 65.00  E-value: 5.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   2 NGD-RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVM 80
Cdd:PRK10841  799 NDDmMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIG 878
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  81 MTAHGsedIAVE---AMKKGAVDYISKPFSSDDMK 112
Cdd:PRK10841  879 VTANA---LAEEkqrCLEAGMDSCLSKPVTLDVLK 910
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
5-183 1.01e-10

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 61.86  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK09836    2 KLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERLQreldeqrqkmaailrgMADMVV-----AVDRQ 159
Cdd:PRK09836   82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIESQFQ----------------VADLMVdlvsrKVTRS 145
                         170       180
                  ....*....|....*....|....*..
gi 2425845196 160 GNVITLNGKAEELLA--IRAE-EVLGR 183
Cdd:PRK09836  146 GTRITLTSKEFTLLEffLRHQgEVLPR 172
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
5-111 1.28e-10

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: 58.56  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEIL--EGESFALVLLDIRMPRMDGMEVLARIRRDYPE---LVVV 79
Cdd:cd19933     2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRrerPLIV 81
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2425845196  80 MMTAHGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:cd19933    82 ALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
379-505 1.66e-10

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 57.78  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 379 FRLLGNLLSNAIKFTPEEGEIEIRAEIvaeplalagplsaaayppanlpvAGRFLLLTVRDTGAGVPADCLVSIFDRFVQ 458
Cdd:cd16923     2 QRVFSNLLSNAIKYSPENTRIYITSFL-----------------------TDDVVNIMFKNPSSHPLDFKLEKLFERFYR 58
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2425845196 459 AKNRRqgKTGGSGLGLAFCRKAMDAHDGFVWAESElDKGSSFHLLFP 505
Cdd:cd16923    59 GDNSR--NTEGAGLGLSIAKAIIELHGGSASAEYD-DNHDLFKVRLP 102
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
146-255 1.68e-10

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 58.19  E-value: 1.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 146 LRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL---QADIPASRLPCrvVLTTGEPCLDVTYVVAQGKR 222
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLppeDAARLERALRR--ALEGEEPIDFLEELLLNGEE 78
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196 223 RlPVLSSATPLRNATGEMIGSVEILHDMSTLKA 255
Cdd:pfam08448  79 R-HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
375-505 2.10e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 57.82  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 375 RSKFFRLLGNLLSNAIKFTPEEGEIEIRAeivaeplalagplsaAAYPpanlpvagRFLLLTVRDTGAGVPADCLVSIFD 454
Cdd:cd16943     1 PSQLNQVLLNLLVNAAQAMEGRGRITIRT---------------WAHV--------DQVLIEVEDTGSGIDPEILGRIFD 57
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2425845196 455 RFVQAKNRRQGktggSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16943    58 PFFTTKPVGEG----TGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
5-90 2.82e-10

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: 57.98  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARI--RRdypELVVVM 80
Cdd:COG2197     3 RVLIVDDHPLVREGLRALLEAEPDIEVvgEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRLltPR---EREVLR 79
                          90
                  ....*....|..
gi 2425845196  81 MTAHG--SEDIA 90
Cdd:COG2197    80 LLAEGlsNKEIA 91
PRK10816 PRK10816
two-component system response regulator PhoP;
5-122 3.03e-10

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 60.14  E-value: 3.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAR 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYN 122
Cdd:PRK10816   82 ESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRN 119
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
6-105 3.41e-10

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: 56.82  E-value: 3.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDyPELVVVMMTAHG 85
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTAKD 79
                          90       100
                  ....*....|....*....|
gi 2425845196  86 SEDIAVEAMKKGAVDYISKP 105
Cdd:cd17621    80 SEIDKVVGLELGADDYVTKP 99
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
6-119 3.50e-10

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 57.42  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:cd17616     1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVeRAI 119
Cdd:cd17616    81 DIEDKVKGLGFGADDYMTKPFHKDELVARI-HAI 113
PAS COG2202
PAS domain [Signal transduction mechanisms];
130-260 4.07e-10

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 60.42  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 130 RLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL-QADIPASRLPCRVVLTTGE 208
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLhPEDRERLLELLRRLLEGGR 206
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196 209 PCLDVTYVVAQGKRRLPVLSSATPLRNATGEMIGSVEILHDMSTLKALEQER 260
Cdd:COG2202   207 ESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK10336 PRK10336
two-component system response regulator QseB;
5-129 4.69e-10

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 59.52  E-value: 4.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAH 84
Cdd:PRK10336    2 RILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWREKGQREPVLILTAR 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2425845196  85 GSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENE 129
Cdd:PRK10336   82 DALAERVEGLRLGADDYLCKPFALIEVAARLEALMRRTNGQASNE 126
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
338-505 5.58e-10

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 61.34  E-value: 5.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 338 LAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivaeplalagpls 417
Cdd:PRK10364  309 LNDLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTAS------------- 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 418 aaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRrqgktgGSGLGLAFCRKAMDAHDGFVWAESELDKG 497
Cdd:PRK10364  376 ----------ESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKAE------GTGLGLAVVHNIVEQHGGTIQVASQEGKG 439

                  ....*...
gi 2425845196 498 SSFHLLFP 505
Cdd:PRK10364  440 ATFTLWLP 447
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
5-107 7.68e-10

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: 56.68  E-value: 7.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17530     2 RVLVLDDDPFQCMMAATILEDLGPGNVDeADDGREALVILLCNAPDIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2425845196  84 HGSedIAVEAMKKGAVDY-------ISKPFS 107
Cdd:cd17530    82 LDG--GILESAETLAGANglnllgtLSKPFS 110
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-488 7.71e-10

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 56.31  E-value: 7.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 380 RLLGNLLSNAIKFTPEEGEIEIRAEIVAEPLAlagplsaaayppanlpvagrfllLTVRDTGAGVPADCLVSIFDRFVQA 459
Cdd:cd16945     7 QAINNLLDNAIDFSPEGGLIALQLEADTEGIE-----------------------LLVFDEGSGIPDYALNRVFERFYSL 63
                          90       100
                  ....*....|....*....|....*....
gi 2425845196 460 KnRRQGKTGGSGLGLAFCRKAMDAHDGFV 488
Cdd:cd16945    64 P-RPHSGQKSTGLGLAFVQEVAQLHGGRI 91
PRK10604 PRK10604
sensor protein RstB; Provisional
314-505 1.02e-09

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 60.39  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 314 MIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRFEpvALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFT 393
Cdd:PRK10604  258 LIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADIQ--AVTPEKTVRLDTPHQGDYGALDMRLMERVLDNLLNNALRYA 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 394 peEGEIEIRaeivaeplalagplsaaayppanLPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGSGLG 473
Cdd:PRK10604  336 --HSRVRVS-----------------------LLLDGNQACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLG 390
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2425845196 474 LAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:PRK10604  391 LAIVHSIALAMGGSVNCDESELGGARFSFSWP 422
PRK15369 PRK15369
two component system response regulator;
1-104 1.08e-09

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 58.17  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIG-YRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVV 78
Cdd:PRK15369    1 MKNYKILLVDDHELIINGIKNMLAPYPrYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNI 80
                          90       100
                  ....*....|....*....|....*.
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISK 104
Cdd:PRK15369   81 LVLTARQEEHMASRTLAAGALGYVLK 106
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
159-251 1.30e-09

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 55.16  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 159 QGNVITLNGKAEELLAIRAEEVLGRPVEELLQADIPASRLPCRVVLTTGEPCLDVTYVVAQGKrRLPVLSSATPLRNATG 238
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREFEVVLYRKDGE-PFPVLVSLAPIRDDGG 79
                          90
                  ....*....|...
gi 2425845196 239 EMIGSVEILHDMS 251
Cdd:pfam13426  80 ELVGIIAILRDIT 92
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
137-508 1.91e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 59.93  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 137 EQRQKMaaiLRGMADMVVAVDRQGNVITLNGKAEELLAIRA---EEVLGRPVEELLqadiPASRLpcRVVLTTGEPCLDV 213
Cdd:PRK11086  221 EQRQAM---LQSIKEGVIAVDDRGEVTLINDEAKRLFNYKKgleDDPLGTDVESWM----PVSRL--KEVLRTGTPRRDE 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 214 TYVVaqgkRRLPVLSSATPLRNaTGEMIGSVEILHDMSTLKALEQEredfvsmlshdlktpITAVVGSIDLVRE------ 287
Cdd:PRK11086  292 EINI----NGRLLLTNTVPVRV-NGEIIGAIATFRDKTEVRQLAQR---------------LDGMVNYADALRAqshefm 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 288 GRLGTINA--EQKEYldsavescDEMVEMIDTLLDVHKFEAGRMQMAIAEEELAPLLRRILSRfepvALRAGIRLFLH-- 363
Cdd:PRK11086  352 NKLHVILGllHLKSY--------DQLEDYILKTANNYQEEIGSLLGKIKSPVIAGFLLGKISR----ARELGITLIISed 419
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 364 --LPPAPilfpvDRSKFFRL---LGNLLSNAIKFTP--EEGEIEIraeivaeplalagplsaaayppaNLPVAGRFLLLT 436
Cdd:PRK11086  420 sqLPDSG-----DEDQVHELitiLGNLIENALEAVGgeEGGEISV-----------------------SLHYRNGWLHCE 471
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 437 VRDTGAGVPADCLVSIFDRFVQAK--NRrqgktggsGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFPMER 508
Cdd:PRK11086  472 VSDDGPGIAPDEIDAIFDKGYSTKgsNR--------GVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQIPWDG 537
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
374-497 2.77e-09

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 54.72  E-value: 2.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEivAEPLAlagplsaaayppanlpvagrflLLTVRDTGAGVPADCLVSIF 453
Cdd:cd16940    10 DALLLFLLLRNLVDNAVRYSPQGSRVEIKLS--ADDGA----------------------VIRVEDNGPGIDEEELEALF 65
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2425845196 454 DRFVQAKNRrqgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKG 497
Cdd:cd16940    66 ERFYRSDGQ---NYGGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
6-120 3.73e-09

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 57.12  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLaRIRRDYPELVVVMMTAHG 85
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFI-RDLRQWSAIPVIVLSARS 82
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2425845196  86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:PRK10529   83 EESDKIAALDAGADDYLSKPFGIGELQARLRVALR 117
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
6-146 7.65e-09

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 58.59  E-value: 7.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196    6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHG 85
Cdd:PRK09959   961 ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLREQNSSLPIWGLTANA 1040
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196   86 SEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRT-----RLENERLQRELDEQRQKMAAIL 146
Cdd:PRK09959  1041 QANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQVAHIapqyrHLDIEALKNNTANDLQLMQEIL 1106
PRK09483 PRK09483
response regulator; Provisional
6-111 1.13e-08

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 55.50  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDI-GYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:PRK09483    4 VLLVDDHELVRAGIRRILEDIkGIKVVgEACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTV 83
                          90       100
                  ....*....|....*....|....*...
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:PRK09483   84 HTENPLPAKVMQAGAAGYLSKGAAPQEV 111
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
149-250 1.29e-08

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 52.64  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 149 MADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL-QADIPASRLPCRVVLTTGEPCLDVTYVVAQGKRRLPVL 227
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIhPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                          90       100
                  ....*....|....*....|...
gi 2425845196 228 SSATPLRNATGEMIGSVEILHDM 250
Cdd:cd00130    81 VSLTPIRDEGGEVIGLLGVVRDI 103
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
425-505 1.74e-08

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 52.40  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 425 NLPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRrqgktgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLF 504
Cdd:cd16920    30 TSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTL 103

                  .
gi 2425845196 505 P 505
Cdd:cd16920   104 P 104
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
5-111 2.38e-08

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 54.65  E-value: 2.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADI--ALILKLQLEDiGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMM 81
Cdd:PRK10651    8 TILLIDDHPMLrtGVKQLISMAP-DITVVgEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVF 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 2425845196  82 TAHGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:PRK10651   87 SVSNHEEDVVTALKRGADGYLLKDMEPEDL 116
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-505 2.91e-08

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 51.66  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 380 RLLGNLLSNAIKFTPEEGEIEIRaeivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQA 459
Cdd:cd16939     3 RALDNLLRNALRYAHRTVRIALL-------------------------VSGGRLTLIVEDDGPGIPAAARERVFEPFVRL 57
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2425845196 460 KNRRQGKTGGSGLGLAFCRKAMDAHDGFVWA-ESELDkGSSFHLLFP 505
Cdd:cd16939    58 DPSRDRATGGFGLGLAIVHRVALWHGGHVECdDSELG-GACFRLTWP 103
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-505 3.16e-08

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.80  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 380 RLLGNLLSNAIKFTPEE-GEIEIRAeivaeplalaGPlsaaayppanlpvAGRFLLLTVRDTGAGVPADCLVSIFDRFVQ 458
Cdd:cd16953     3 QVLRNLIGNAISFSPPDtGRITVSA----------MP-------------TGKMVTISVEDEGPGIPQEKLESIFDRFYT 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2425845196 459 AKNRRQGKTGGSGLGLAFCRKAMDAHDGFVWAESELD----KGSSFHLLFP 505
Cdd:cd16953    60 ERPANEAFGQHSGLGLSISRQIIEAHGGISVAENHNQpgqvIGARFTVQLP 110
PRK14084 PRK14084
DNA-binding response regulator;
5-119 3.46e-08

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 54.37  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:PRK14084    2 KALIVDDEPLARNELTYLLNEIGGFEEinEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKIQKMKEPPAIIFAT 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  83 AHgsEDIAVEAMKKGAVDYISKPFSSDdmkgRVERAI 119
Cdd:PRK14084   82 AH--DQFAVKAFELNATDYILKPFEQK----RIEQAV 112
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
384-492 3.55e-08

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 51.63  E-value: 3.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 384 NLLSNAIKFTPEE-GEIEIRAEiVAEPLALAGPlsaaayppanlpvagRF---LLLTVRDTGAGVPADCLVSIFDRFVQa 459
Cdd:cd16918     7 NLVRNAAQALAGSgGEIILRTR-TQRQVTLGHP---------------RHrlaLRVSVIDNGPGIPPDLQDTIFYPMVS- 69
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196 460 knrrqGKTGGSGLGLAFCRKAMDAHDGFVWAES 492
Cdd:cd16918    70 -----GRENGTGLGLAIAQNIVSQHGGVIECDS 97
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
6-105 4.36e-08

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 51.22  E-value: 4.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-----RDYPelvVVM 80
Cdd:cd17602     1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRkssalKDTP---IIM 77
                          90       100
                  ....*....|....*....|....*
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd17602    78 LTGKDGLVDRIRAKMAGASGYLTKP 102
PRK13435 PRK13435
response regulator; Provisional
5-130 4.99e-08

response regulator; Provisional


Pssm-ID: 184052 [Multi-domain]  Cd Length: 145  Bit Score: 51.98  E-value: 4.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRMPR-MDGMEVLARIRRDYpELVVVMMT 82
Cdd:PRK13435    7 KVLIVEDEALIALELEKLVEEAGHEVVgIAMSSEQAIALGRRRQPDVALVDVHLADgPTGVEVARRLSADG-GVEVVFMT 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2425845196  83 AH---GSEDIAveamkkGAVDYISKPFSSDdmkgRVERAIQYNRTRLENER 130
Cdd:PRK13435   86 GNperVPHDFA------GALGVIAKPYSPR----GVARALSYLSARRVGDR 126
PRK10337 PRK10337
sensor protein QseC; Provisional
248-485 5.66e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 55.04  E-value: 5.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 248 HDMstlkaLEQEREdFVSMLSHDLKTPITAVVGSIDLVRegrLGTINAEQKEY----LDSAVescDEMVEMIDTLLDVHK 323
Cdd:PRK10337  231 HAM-----MVRERR-FTSDAAHELRSPLAALKVQTEVAQ---LSDDDPQARKKallqLHAGI---DRATRLVDQLLTLSR 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 324 FEAGRMQMAIAEEELAPLLRRILSRFEPVALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRa 403
Cdd:PRK10337  299 LDSLDNLQDVAEIPLEDLLQSAVMDIYHTAQQAGIDVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVT- 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 404 eivaeplalagpLSAAAyppanlpvagrfllLTVRDTGAGVPADCLVSIFDRFVQAKNrrQGKTgGSGLGLAFCRKAMDA 483
Cdd:PRK10337  378 ------------LNARN--------------FTVRDNGPGVTPEALARIGERFYRPPG--QEAT-GSGLGLSIVRRIAKL 428

                  ..
gi 2425845196 484 HD 485
Cdd:PRK10337  429 HG 430
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
110-259 1.11e-07

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 54.68  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  110 DMKGRVERAIQYNRTRLENERLQRELDEQRQKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL 189
Cdd:PRK09776   506 NKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVL 585
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196  190 Q------ADIPASRLPCRVVLTTGEPCLDVTYVVAQGKRrLPVLSSATPLRNATGEMIGSVEILHDMSTLKALEQE 259
Cdd:PRK09776   586 HitfgdnGPLMENIYSCLTSRSAAYLEQDVVLHCRSGGS-YDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQ 660
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
5-107 1.45e-07

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 54.18  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYP--ELV-VVMM 81
Cdd:PRK11091  527 NILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPreDLPpLVAL 606
                          90       100
                  ....*....|....*....|....*.
gi 2425845196  82 TAHGSEDiAVEAMKKGAVDYISKPFS 107
Cdd:PRK11091  607 TANVLKD-KKEYLDAGMDDVLSKPLS 631
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
239-491 2.02e-07

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 53.40  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 239 EMIGSVEILhdMSTlkaleQERedFVSMLSHDLKTPITAVVGSIDLVREgRLGtinaEQKEY--LDSAVESCDEMvemID 316
Cdd:PRK09470  231 QMVTALERM--MTS-----QQR--LLSDISHELRTPLTRLQLATALLRR-RQG----ESKELerIETEAQRLDSM---IN 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 317 TLLdvhkfEAGRMQMAIAEE-ELAP---LLRRIL--SRFEpvALRAGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAI 390
Cdd:PRK09470  294 DLL-----VLSRNQQKNHLErETFKansLWSEVLedAKFE--AEQMGKSLTVSAPPGPWPINGNPNALASALENIVRNAL 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 391 KFTPEEGEIEIRAEivaeplalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRRQGKTGGS 470
Cdd:PRK09470  367 RYSHTKIEVAFSVD-------------------------KDGLTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGT 421
                         250       260
                  ....*....|....*....|.
gi 2425845196 471 GLGLAFCRKAMDAHDGFVWAE 491
Cdd:PRK09470  422 GLGLAIVENAIQQHRGWVKAE 442
PRK10693 PRK10693
two-component system response regulator RssB;
33-147 2.24e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 52.69  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  33 ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGS-EDIAvEAMKKGAVDYISKPFSSddm 111
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENmADIA-KALRLGVQDVLLKPVKD--- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2425845196 112 kgrveraiqYNRTR----------------LENERLQRELDEQRQKMAAILR 147
Cdd:PRK10693   79 ---------LNRLRemvfaclypsmfnsrvEEEERLFRDWDALVDNPAAAAK 121
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
6-105 2.33e-07

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: 48.81  E-value: 2.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd17565     1 FYIVDDDKNIIKILSDIIEDDDLGEVvgEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQLVRKLKDTGSNGKFIMISQ 80
                          90       100
                  ....*....|....*....|..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKP 105
Cdd:cd17565    81 VSDKEMIGKAYQAGIEFFINKP 102
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
6-106 2.60e-07

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. 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. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 49.01  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAhg 85
Cdd:cd19922     1 ILLLEKERNLAHFLSLELQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKLSRIKPASVIIVLDH-- 78
                          90       100
                  ....*....|....*....|...
gi 2425845196  86 SEDIA--VEAMKKGAVDYISKPF 106
Cdd:cd19922    79 WEDLQeeLEEVQRFAVSYVVKPV 101
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
380-486 3.43e-07

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: 48.60  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 380 RLLGNLLSNAIKFTpeEGEIEIRAEivaeplalagplsaaayppanlpVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQA 459
Cdd:cd16950     3 RVLSNLVDNALRYG--GGWVEVSSD-----------------------GEGNRTRIQVLDNGPGIAPEEVDELFQPFYRG 57
                          90       100
                  ....*....|....*....|....*..
gi 2425845196 460 KNRRqgKTGGSGLGLAFCRKAMDAHDG 486
Cdd:cd16950    58 DNAR--GTSGTGLGLAIVQRISDAHGG 82
PRK13557 PRK13557
histidine kinase; Provisional
382-505 4.90e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 52.37  E-value: 4.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTPEEGEIEIRAEIVaeplaLAGPLSAAAYPPanlPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKN 461
Cdd:PRK13557  282 LLNVLINARDAMPEGGRVTIRTRNV-----EIEDEDLAMYHG---LPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKE 353
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2425845196 462 rrQGKtgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:PRK13557  354 --EGK--GTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP 393
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
5-125 5.05e-07

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: 48.77  E-value: 5.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEAD--------IALILKLQLEDIGYR-TVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPE 75
Cdd:cd17533     2 NIFILEDDKIqrvrleeiIENILKIENIEYVIElTGKTEELLEKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDPY 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196  76 LVVVMMTAHgSE------DIAVEAMkkgavDYISKPFSSDDMKGRVERAIQYNRTR 125
Cdd:cd17533    82 AIIIFVTTH-SEfapltfEYKVAAL-----DFILKPLKLEEFKKRIEECIKYAQKN 131
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
382-505 5.90e-07

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: 48.05  E-value: 5.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 382 LGNLLSNAIKFTPEEG------EIEIRAEivaeplalagplsaaayppanlpvaGRFLLLTVRDTGAGVPADCLVSIFDR 455
Cdd:cd16915     5 VGNLIDNALDALAATGapnkqvEVFLRDE-------------------------GDDLVIEVRDTGPGIAPELRDKVFER 59
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2425845196 456 FVQAKnrrqgKTGGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHLLFP 505
Cdd:cd16915    60 GVSTK-----GQGERGIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
PRK11697 PRK11697
two-component system response regulator BtsR;
5-138 5.98e-07

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 50.62  E-value: 5.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRrdyPELV--VVM 80
Cdd:PRK11697    3 KVLIVDDEPLAREELRELLQEEGDIEIvgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLD---PEHMpyIVF 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  81 MTAHgsEDIAVEAMKKGAVDYISKPfssddmkgrVERAiqynrtRLEN--ERLQRELDEQ 138
Cdd:PRK11697   80 VTAF--DEYAIKAFEEHAFDYLLKP---------IDPA------RLAKtlARLRQERSPQ 122
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
144-260 7.95e-07

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 48.06  E-value: 7.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 144 AILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQA-DIPASRLPCRVVLtTGEPCLDVTYVVAQGK- 221
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEeDREEVRERIERRL-EGEPEPVSEERRVRRKd 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2425845196 222 -RRLPVLSSATPLRnATGEMIGSVEILHDMSTLKALEQER 260
Cdd:TIGR00229  86 gSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEEAL 124
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
140-189 1.68e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.47  E-value: 1.68e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2425845196  140 QKMAAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELL 189
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
5-105 1.71e-06

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 51.00  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDD-EADIALI---LKLQLEDIgyrtVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-----RDYPe 75
Cdd:PRK11107  669 TVMAVDDnPANLKLIgalLEEQVEHV----VLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRqlphnQNTP- 743
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196  76 lvVVMMTAHGsedIAVEA---MKKGAVDYISKP 105
Cdd:PRK11107  744 --IIAVTAHA---MAGERerlLSAGMDDYLAKP 771
PRK10360 PRK10360
transcriptional regulator UhpA;
36-111 2.79e-06

transcriptional regulator UhpA;


Pssm-ID: 182408 [Multi-domain]  Cd Length: 196  Bit Score: 48.05  E-value: 2.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196  36 GAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDypeLVVVMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDM 111
Cdd:PRK10360   36 GREALAGLPGRGVQVCICDISMPDISGLELLSQLPKG---MATIMLSVHDSPALVEQALNAGARGFLSKRCSPDEL 108
PRK10430 PRK10430
two-component system response regulator DcuR;
6-140 3.25e-06

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 48.57  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDI-GYR---TVRARDGAEALeILEGE-SFALVLLDIRMPRMDGMEVLARIRRDYPELVVVM 80
Cdd:PRK10430    4 VLIVDDDAMVAELNRRYVAQIpGFQccgTASTLEQAKEI-IFNSDtPIDLILLDIYMQQENGLDLLPVLHEAGCKSDVIV 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  81 MTAHGSEDIAVEAMKKGAVDYISKPFSSddmkGRVERAiqynrtrLENERLQRELDEQRQ 140
Cdd:PRK10430   83 ISSAADAATIKDSLHYGVVDYLIKPFQA----SRFEEA-------LTGWRQKKMALEKHQ 131
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
6-120 3.31e-06

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: 46.19  E-value: 3.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLE-DIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTA 83
Cdd:cd19931     1 VLLIDDHPLLRKGIKQLIElDPDFTVVgEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILTV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd19931    81 SDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQAAS 117
dpiA PRK10046
two-component response regulator DpiA; Provisional
6-219 8.02e-06

two-component response regulator DpiA; Provisional


Pssm-ID: 182208 [Multi-domain]  Cd Length: 225  Bit Score: 46.93  E-value: 8.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDI-GYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRD-YPELVVVMMT 82
Cdd:PRK10046    7 LLIVEDETPLAEMHAEYIRHIpGFSQIlLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAhYPGDVVFTTA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  83 AHGSEDIAvEAMKKGAVDYISKPFSSDDMKGRVERAIQYNRTRLENERL-QRELDEQrqkMAAILRG--MADMVVAVDrq 159
Cdd:PRK10046   87 ASDMETVS-EAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESIDSAsQKQIDEM---FNAYARGepKDELPTGID-- 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 160 gnVITLNGkaeeLLAIRAEEVLGRPVEELLQAdIPASRLPCRVVLttgEPCLDVTYVVAQ 219
Cdd:PRK10046  161 --PLTLNA----VRKLFKEPGVQHTAETVAQA-LTISRTTARRYL---EYCASRHLIIAE 210
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
255-486 8.17e-06

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 48.04  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 255 ALEQEREdFVSMLSHDLKTPITAVVGSIDLVregrlgtinaEQKEYLDSA--VESCDEMVEMIDTLLDV----HKFEAGR 328
Cdd:PRK10755  133 TLDQERL-FTADVAHELRTPLAGIRLHLELL----------EKQHHIDVAplIARLDQMMHTVEQLLQLaragQSFSSGH 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 329 MQ-MAIAEEELAPLlRRILSrfEPVALRaGIRLFLHLPPAPILFPVDRSKFFRLLGNLLSNAIKFTPEEGEIEIRaeiva 407
Cdd:PRK10755  202 YQtVKLLEDVILPS-QDELS--EMLEQR-QQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIK----- 272
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2425845196 408 eplalagplsaaayppanLPVAGRFLLLTVRDTGAGVPADCLVSIFDRFVQAKNRrqgkTGGSGLGLAFCRKAMDAHDG 486
Cdd:PRK10755  273 ------------------LSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMDSR----YGGIGLGLSIVSRITQLHHG 329
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
5-120 2.21e-05

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: 43.78  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTVR-ARDGAEALEILEGESFALVLLDIRMP-RMDGMEVLARIR--RDYPelvVVM 80
Cdd:cd17540     2 RVLIIEDEPLIAMDLEQIVEDLGHQVVGiARTRDEAVALARRERPDLILADIQLAdGSSGIDAVNEILttHDVP---VIF 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2425845196  81 MTAHGsediavEAMKKGA----VDYISKPFSSDDMKGRVERAIQ 120
Cdd:cd17540    79 VTAYP------ERLLTGErpepTFLITKPFDPEMVKAAISQALF 116
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
429-502 2.58e-05

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: 43.21  E-value: 2.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2425845196 429 AGRfLLLTVRDTGAGVPADCLVSIFDRFVQAKNrrQGKtgGSGLGLAFCRKAMDAHDGFVWAESELDKGSSFHL 502
Cdd:cd16976    32 GGR-LVLVVRDNGPGIAEEHLSRVFDPFFTTKP--VGK--GTGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
PRK09191 PRK09191
two-component response regulator; Provisional
5-125 5.10e-05

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 44.84  E-value: 5.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLEDIGYRTV-RARDGAEALEILEGESFALVLLDIRM-PRMDGMEVLARIRRDYpELVVVMMT 82
Cdd:PRK09191  139 RVLIIEDEPIIAMDLEQLVESLGHRVTgIARTRAEAVALAKKTRPGLILADIQLaDGSSGIDAVNDILKTF-DVPVIFIT 217
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2425845196  83 AHGSEDIAVEAMKKGAVdyISKPFSSDDMKGRVERAIQYNRTR 125
Cdd:PRK09191  218 AFPERLLTGERPEPAFL--ITKPFQPDTVKAAISQALFFQETE 258
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
1-104 6.66e-05

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 44.24  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNgdRILIVDDEADIA-LILK-LQLEDIGYrTVRARdGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPElVV 78
Cdd:PRK10701    1 MN--KIVFVEDDAEVGsLIAAyLAKHDIDV-TVEPR-GDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQG-PI 75
                          90       100
                  ....*....|....*....|....*.
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISK 104
Cdd:PRK10701   76 VLLTSLDSDMNHILALEMGACDYILK 101
PRK13856 PRK13856
two-component response regulator VirG; Provisional
6-120 6.93e-05

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 44.42  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARI--RRDYPelVVVMMTA 83
Cdd:PRK13856    4 VLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGLEIVRSLatKSDVP--IIIISGD 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2425845196  84 HGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVERAIQ 120
Cdd:PRK13856   82 RLEEADKVVALELGATDFIAKPFGTREFLARIRVALR 118
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
129-190 7.75e-05

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 45.18  E-value: 7.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2425845196 129 ERLQRELDeqrqkmaAILRGMADMVVAVDRQGNVITLNGKAEELLAIRAEEVLGRPVEELLQ 190
Cdd:COG3283    76 EREHLELD-------ALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLSELLK 130
PRK13558 PRK13558
bacterio-opsin activator; Provisional
33-183 8.19e-05

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.21  E-value: 8.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  33 ARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMTAHGSEDIAVEAMKKGAVDYIskPFSSDDMK 112
Cdd:PRK13558   37 IRDFVAARDRVEAGEIDCVVADHEPDGFDGLALLEAVRQTTAVPPVVVVPTAGDEAVARRAVDADAAAYV--PAVSDDAT 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 113 GRV----------------ERAIQYNRTRLENERL-QRELDEqrqkmAAILRGMADmvvAVDRQGNVITLNGKAEELLAI 175
Cdd:PRK13558  115 AAIaeriesavpehsrdteARMPISDLTVESDRRLkERALDE-----APVGITIAD---ATLPDEPLIYINDAFERITGY 186

                  ....*...
gi 2425845196 176 RAEEVLGR 183
Cdd:PRK13558  187 SPDEVLGR 194
PRK13560 PRK13560
hypothetical protein; Provisional
71-259 1.63e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 44.28  E-value: 1.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196  71 RDYPELVVVMMTAHGSEDIAVEAMKKGA----VDYISKPFSSDDMKGRVERAIQYNRTRLENERLQRELDEQRQKMAAIL 146
Cdd:PRK13560  259 DDYQEADAAKFDADGSQIIEAEFQNKDGrtrpVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAII 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 147 RGMADMVVAVDRQGNVITL-NGKAEELLAIRAEEVLGRPV--------EELLQADIPASRLPCRVVLTTGEPcldVTYVV 217
Cdd:PRK13560  339 EAAPIAAIGLDADGNICFVnNNAAERMLGWSAAEVMGKPLpgmdpelnEEFWCGDFQEWYPDGRPMAFDACP---MAKTI 415
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196 218 AQGKR--------------RLPVLSSATPLRNATGEMIGSVEILHDMSTLKALEQE 259
Cdd:PRK13560  416 KGGKIfdgqevliereddgPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQ 471
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
1-84 1.65e-04

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 44.51  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTVRARDGAEALEIL-EGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVV 79
Cdd:PRK11466  679 LDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLqNSEPFAAALVDFDLPDYDGITLARQLAQQYPSLVLI 758

                  ....*
gi 2425845196  80 MMTAH 84
Cdd:PRK11466  759 GFSAH 763
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
6-112 4.69e-04

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: 40.04  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   6 ILIVDDE-ADIALILKLqLEDIGYRTVRARDGAEALEIL--EGESFA---------LVLLDIRMPRMDGMEVLARIRRDY 73
Cdd:cd17581     1 VLAVDDSlVDRKVIERL-LRISSCRVTAVDSGKRALEFLglEDEEDSsnfnepkvnMIITDYCMPGMTGYDLLKKVKESS 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2425845196  74 P--ELVVVMMTahgSEDIAV---EAMKKGAVDYISKPFSSDDMK 112
Cdd:cd17581    80 AlkEIPVVIMS---SENIPTrisRCLEEGAEDFLLKPVKLADVK 120
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
5-104 4.87e-04

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 41.76  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQLE-DIGYRTV-RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVVVMMT 82
Cdd:PRK10403    8 QVLIVDDHPLMRRGVRQLLElDPGFEVVaEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQIIILT 87
                          90       100
                  ....*....|....*....|..
gi 2425845196  83 AHGSEDIAVEAMKKGAVDYISK 104
Cdd:PRK10403   88 VSDASSDVFALIDAGADGYLLK 109
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
5-104 1.05e-03

first 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 contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the first REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381148 [Multi-domain]  Cd Length: 115  Bit Score: 38.70  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILK-LQLEDIGYRTVRARDGAEALEILEGES-FALVLLDIRMPrmdgmevlarirrDYP--ELV--- 77
Cdd:cd19921     1 KVLIVEDSKTFSKVLKhLIAQELGLEVDVAETLAEAKALLEEGDdYFAALVDLNLP-------------DAPngEAVdlv 67
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2425845196  78 ------VVMMTAHGSEDIAVEAMKKGAVDYISK 104
Cdd:cd19921    68 lekgipVIVLTGSFDEDKRETLLSKGVVDYVLK 100
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
263-508 1.44e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 41.16  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 263 FVSMLSHDLKTPITAVVGSIDLVREGRLGTINAEQKEYLDSAVESCDEMVEMIDTLLDVHK----------FEAGRMQM- 331
Cdd:COG2972   173 LSYLLSRSITRPIKRLKKAMKKVEKGDLVRLEVSGNDEIGILARSFNEMVERIKELIEEVYelelekkeaeLKALQAQIn 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 332 ---------AIAE--------------EELAPLLRRILSRFE---PVA--------------LRAG--IRLFLHLPPAPI 369
Cdd:COG2972   253 phflfntlnSIRWlaeledpeeaeemlEALSKLLRYSLSKGDelvTLEeeleliksyleiqkLRFGdrLEVEIEIDEELL 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 370 LFPVdrskFFRLLGNLLSNAIK--FTP--EEGEIEIRAEIvaeplalagplsaaayppanlpvAGRFLLLTVRDTGAGVP 445
Cdd:COG2972   333 DLLI----PKLILQPLVENAIEhgIEPkeGGGTIRISIRK-----------------------EGDRLVITVEDNGVGMP 385
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2425845196 446 ADCLVSIFDRFvqaknrrQGKTGGSGLGLAFCRKAMDAHDG---FVWAESELDKGSSFHLLFPMER 508
Cdd:COG2972   386 EEKLEKLLEEL-------SSKGEGRGIGLRNVRERLKLYYGeeyGLEIESEPGEGTTVTIRIPLEE 444
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
374-491 2.12e-03

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


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 37.83  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196 374 DRSKFFRLLGNLLSNAIKFTPEEGEIEIRAEIVAEplalagplsaaayppanlpvagrFLLLTVRDTGAGVPADCLVSIF 453
Cdd:cd16975     1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEE-----------------------YLYFEIWDNGHGFSEQDLKKAL 57
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2425845196 454 DRFVQAKNRRQGKtGGSGLGLAFCRKAMDAHDGFVWAE 491
Cdd:cd16975    58 ELFYRDDTSRRSG-GHYGMGLYIAKNLVEKHGGSLIIE 94
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
1-116 2.44e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.47  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   1 MNGDRILIVDDEADIALILKLQLEDIGYRTV--RARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIRRDYPELVV 78
Cdd:PRK09935    1 MKPASVIIMDTHPIIRMSIEVLLQKNSELQIvlKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQSTVKV 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2425845196  79 VMMTAHGSEDIAVEAMKKGAVDYISKPFSSDDMKGRVE 116
Cdd:PRK09935   81 LFLSSKSECFYAGRAIQAGANGFVSKCNDQNDIFHAVQ 118
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
5-104 5.50e-03

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


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 37.00  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2425845196   5 RILIVDDEADIALILKLQL---EDIGYRTvrARDGAEALEILEGESFALVLLDIRMPRMDGMEVLARIR-----RDYPel 76
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALadeEDIDFHY--CSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRanpatRDIP-- 77
                          90       100
                  ....*....|....*....|....*...
gi 2425845196  77 VVVMMTAHGSEdIAVEAMKKGAVDYISK 104
Cdd:cd17575    78 IIVLSTKEEPE-VKSEAFALGANDYLVK 104
 
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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