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Conserved domains on  [gi|639298814|ref|WP_024589456|]
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MULTISPECIES: response regulator [Pseudoalteromonas]

Protein Classification

ATP-binding protein( domain architecture ID 1002581)

ATP-binding protein similar to the ATPase domains of hybrid sensor kinases that regulate diverse biological functions through distinct molecular mechanisms

CATH:  3.30.565.10
EC:  2.7.13.3
Gene Ontology:  GO:0000155|GO:0005524
PubMed:  10966457
SCOP:  4001957

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMAO_torS super family cl37193
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
219-709 1.03e-83

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


The actual alignment was detected with superfamily member TIGR02956:

Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 285.13  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  219 KLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEA 298
Cdd:TIGR02956 452 KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  299 LYEEDVEFKTWLNNLCLLLSPLAEQKQLkfELICNIPEQ--ACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVDLvle 376
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGI--QLRLNIPEQlpNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--- 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  377 kQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTVTFTL 456
Cdd:TIGR02956 607 -NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  457 GELSLVEQRHQTKDyLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEV 536
Cdd:TIGR02956 686 GKPAEDSATLTVID-LPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTL 764
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  537 LKRLKRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKL----RQALSDSQSNQTA-------------- 598
Cdd:TIGR02956 765 LQQLRAIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLtamiAVILAGGKSNTEApvlsaspsfdsasv 844
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  599 ---------SIAVELIDTLYDKTAAETLTSSFSEDEVSSIYNEFVLSARNKLIRCQKLID-QQPEQCIKLLHRQASTALQ 668
Cdd:TIGR02956 845 ienaqaddiPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAvDDDAQIKKLAHKLKGSAGS 924
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 639298814  669 LGFNRYGIELKKIERRLLDKKPHNDMLDEALDLWQRS---LEQY 709
Cdd:TIGR02956 925 LGLTQLTQLCQQLEKQGKTGALELSDIDEIKQAWQASktaLDQW 968
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
219-709 1.03e-83

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 285.13  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  219 KLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEA 298
Cdd:TIGR02956 452 KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  299 LYEEDVEFKTWLNNLCLLLSPLAEQKQLkfELICNIPEQ--ACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVDLvle 376
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGI--QLRLNIPEQlpNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--- 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  377 kQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTVTFTL 456
Cdd:TIGR02956 607 -NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  457 GELSLVEQRHQTKDyLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEV 536
Cdd:TIGR02956 686 GKPAEDSATLTVID-LPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTL 764
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  537 LKRLKRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKL----RQALSDSQSNQTA-------------- 598
Cdd:TIGR02956 765 LQQLRAIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLtamiAVILAGGKSNTEApvlsaspsfdsasv 844
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  599 ---------SIAVELIDTLYDKTAAETLTSSFSEDEVSSIYNEFVLSARNKLIRCQKLID-QQPEQCIKLLHRQASTALQ 668
Cdd:TIGR02956 845 ienaqaddiPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAvDDDAQIKKLAHKLKGSAGS 924
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 639298814  669 LGFNRYGIELKKIERRLLDKKPHNDMLDEALDLWQRS---LEQY 709
Cdd:TIGR02956 925 LGLTQLTQLCQQLEKQGKTGALELSDIDEIKQAWQASktaLDQW 968
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
213-591 2.35e-60

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 217.12  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 213 REQHLNKLaDKAQKDleiRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASL 292
Cdd:PRK11091 269 RKRYQDAL-EKASRD---KTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKM 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 293 DQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELICNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVd 372
Cdd:PRK11091 345 ERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV- 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 373 lvlEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ---SSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFS 449
Cdd:PRK11091 424 ---RYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQvkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFT 500
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 450 FTVTFTLGELSLVEQRHQTKDYLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLP 529
Cdd:PRK11091 501 LTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLP 580
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298814 530 DLTGQEVLKRLKRIDHKNQRTPVLAFTASLSPDEvKEYLELGIKDIVGKPIKHEKLRQALSD 591
Cdd:PRK11091 581 DMTGLDIARELRERYPREDLPPLVALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKK 641
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
121-451 1.63e-58

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 201.29  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 121 VIASDIQHIAEAGFLLFIFIKCARKPYPNGSIVYITILTLVALSFIGRSLFMDNIEQKNLLVNGWFSSLLFLNGVIAPMF 200
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 201 YAAGMALLcnERREQHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKaYCEAIINSAESLN 280
Cdd:COG0642   82 LLLLLLLL--LLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQRE-YLETILRSADRLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 281 LLVDKVLDYASLDQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELicNIPEQACY-YCDQQKLRQIIINLVGNAI 359
Cdd:COG0642  159 RLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL--DLPDDLPTvRGDPDRLRQVLLNLLSNAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 360 KFTDHGTvKIQVDLVLEkqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIA 439
Cdd:COG0642  237 KYTPEGG-TVTVSVRRE---GDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVE 312
                        330
                 ....*....|..
gi 639298814 440 SQLGTGSVFSFT 451
Cdd:COG0642  313 SEPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
347-454 1.12e-33

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


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 124.53  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVKIQVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ--SSAGKEKGGTGLGLAI 424
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQadSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 425 TSRLLEKLSSRLEIASQLGTGSVFSFTVTF 454
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
343-452 4.54e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 100.03  E-value: 4.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814   343 DQQKLRQIIINLVGNAIKFT-DHGTVKIQVDLVlekqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEK-GGTGL 420
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-----GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKiGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 639298814   421 GLAITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
477-589 3.04e-22

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 92.21  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFT 556
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT---TPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 639298814  557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
215-454 3.35e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.12  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 215 QHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVmnqtSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQ 294
Cdd:NF012163 224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI----QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSM 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 295 SDE-ALyeedVEFKTWLNNLCLLLSPLA------EQKQLKFELicNIPEQACYYCDQQKLRQIIINLVGNAIKFTDH-GT 366
Cdd:NF012163 300 SDEgAL----AYQKASVDLVPLLEVEGGafrerfASAGLELEV--SLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSgGS 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 367 VKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIA-SQLG 443
Cdd:NF012163 374 LHISA-----SQRPKEVTLTVADSAPGVSDEQLARLFERFyrVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLG 448
                        250
                 ....*....|.
gi 639298814 444 TGSVfsfTVTF 454
Cdd:NF012163 449 GLRI---VVTL 456
ActS_PrrB_HisK NF033792
ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, ...
353-439 1.55e-06

ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, found in alpha-proteobacteria, shows strong sequence conservation, including the notable motif [VA]AAAAHELGTPxTI. It always acts as a partner to an ActR/PrrA/RegA family global response regulator transcription factor in a two-component sensory transduction system. Lineage-specific names and gene symbols given to this histidine kinase reflect downstream regulator changes such as entry into stationary phase, anaerobic expression of photosynthesis genes, and survival of exposure to low pH.


Pssm-ID: 468186 [Multi-domain]  Cd Length: 423  Bit Score: 50.98  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 353 NLVGNAIKF-TDHGTVKIQVDlvlekqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEK----GGTGLGLAITSR 427
Cdd:NF033792 318 NLIENAVDFaRSTVTVTASWD-------AESVTITIEDDGPGFPPDVLSRIGEPYVTTRRGEERrpggGGLGLGLFIAKT 390
                         90
                 ....*....|..
gi 639298814 428 LLEKLSSRLEIA 439
Cdd:NF033792 391 LLERSGATVTFA 402
 
Name Accession Description Interval E-value
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
219-709 1.03e-83

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 285.13  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  219 KLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEA 298
Cdd:TIGR02956 452 KARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  299 LYEEDVEFKTWLNNLCLLLSPLAEQKQLkfELICNIPEQ--ACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVDLvle 376
Cdd:TIGR02956 532 ISPRPFDLNALLDDVHHLMVSRAQLKGI--QLRLNIPEQlpNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL--- 606
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  377 kQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTVTFTL 456
Cdd:TIGR02956 607 -NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  457 GELSLVEQRHQTKDyLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEV 536
Cdd:TIGR02956 686 GKPAEDSATLTVID-LPPQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTL 764
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  537 LKRLKRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKL----RQALSDSQSNQTA-------------- 598
Cdd:TIGR02956 765 LQQLRAIYGAKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLtamiAVILAGGKSNTEApvlsaspsfdsasv 844
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  599 ---------SIAVELIDTLYDKTAAETLTSSFSEDEVSSIYNEFVLSARNKLIRCQKLID-QQPEQCIKLLHRQASTALQ 668
Cdd:TIGR02956 845 ienaqaddiPESNQASEFLLDEEQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAvDDDAQIKKLAHKLKGSAGS 924
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 639298814  669 LGFNRYGIELKKIERRLLDKKPHNDMLDEALDLWQRS---LEQY 709
Cdd:TIGR02956 925 LGLTQLTQLCQQLEKQGKTGALELSDIDEIKQAWQASktaLDQW 968
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
213-591 2.35e-60

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 217.12  E-value: 2.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 213 REQHLNKLaDKAQKDleiRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASL 292
Cdd:PRK11091 269 RKRYQDAL-EKASRD---KTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKM 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 293 DQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELICNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVd 372
Cdd:PRK11091 345 ERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV- 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 373 lvlEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ---SSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFS 449
Cdd:PRK11091 424 ---RYEEGDMLTFEVEDSGIGIPEDELDKIFAMYYQvkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFT 500
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 450 FTVTFTLGELSLVEQRHQTKDYLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLP 529
Cdd:PRK11091 501 LTIHAPAVAEEVEDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLP 580
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298814 530 DLTGQEVLKRLKRIDHKNQRTPVLAFTASLSPDEvKEYLELGIKDIVGKPIKHEKLRQALSD 591
Cdd:PRK11091 581 DMTGLDIARELRERYPREDLPPLVALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKK 641
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
121-451 1.63e-58

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 201.29  E-value: 1.63e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 121 VIASDIQHIAEAGFLLFIFIKCARKPYPNGSIVYITILTLVALSFIGRSLFMDNIEQKNLLVNGWFSSLLFLNGVIAPMF 200
Cdd:COG0642    2 LLLLLLLVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 201 YAAGMALLcnERREQHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKaYCEAIINSAESLN 280
Cdd:COG0642   82 LLLLLLLL--LLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQRE-YLETILRSADRLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 281 LLVDKVLDYASLDQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELicNIPEQACY-YCDQQKLRQIIINLVGNAI 359
Cdd:COG0642  159 RLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELEL--DLPDDLPTvRGDPDRLRQVLLNLLSNAI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 360 KFTDHGTvKIQVDLVLEkqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIA 439
Cdd:COG0642  237 KYTPEGG-TVTVSVRRE---GDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVE 312
                        330
                 ....*....|..
gi 639298814 440 SQLGTGSVFSFT 451
Cdd:COG0642  313 SEPGKGTTFTVT 324
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
216-452 1.94e-53

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 184.34  E-value: 1.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 216 HLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKA--YCEAIINSAESLNLLVDKVLDYASLD 293
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEERreLLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 294 QSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELicNIPEQACY-YCDQQKLRQIIINLVGNAIKFT-DHGTVKIQV 371
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLEL--DLPPELPLvYADPELLEQVLANLLDNAIKYSpPGGTITISA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 372 dlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:COG2205  159 -----RREGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233

                 .
gi 639298814 452 V 452
Cdd:COG2205  234 L 234
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
152-451 1.88e-51

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 183.60  E-value: 1.88e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 152 IVYITILTLVALSFIGRSLFMDNIEQKNLLVNGWFSSLLFLNGVIAPMFYAAGMALLCNERREQHLNKL--ADKAQKDle 229
Cdd:COG5002   90 LLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELerLEQMRRE-- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 230 irglFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKA--YCEAIINSAESLNLLVDKVLDYASLDQSDEALYEEDVEFK 307
Cdd:COG5002  168 ----FVANVSHELRTPLTSIRGYLELLLDGAADDPEERreYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 308 TWLNNLCLLLSPLAEQKQLKFELicNIPEQACY-YCDQQKLRQIIINLVGNAIKFT-DHGTVKIQVdlvleKQLEHTIKI 385
Cdd:COG5002  244 ELLEEVVEELRPLAEEKGIELEL--DLPEDPLLvLGDPDRLEQVLTNLLDNAIKYTpEGGTITVSL-----REEDDQVRI 316
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 386 SVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:COG5002  317 SVRDTGIGIPEEDLPRIFERFyrVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTIT 384
PRK15347 PRK15347
two component system sensor kinase;
213-590 6.67e-49

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 185.23  E-value: 6.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 213 REQHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASL 292
Cdd:PRK15347 380 RTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRI 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 293 DQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELICN--IPEQAcyYCDQQKLRQIIINLVGNAIKFTDHGTVKIQ 370
Cdd:PRK15347 460 ESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGahVPLYL--HLDSLRLRQILVNLLGNAVKFTETGGIRLR 537
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 371 VdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAgkEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSF 450
Cdd:PRK15347 538 V-----KRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADT--HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSL 610
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 451 TVTFT---------------------------LGELSLVEQRHQTKD--YLTG--------------------------- 474
Cdd:PRK15347 611 VLPLNeyappeplkgelsaplalhrqlsawgiTCQPGHQNPALLDPElaYLPGrlydllqqiiqgapnepvinlplqpwq 690
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLkRLKRIDHKNQRT--PV 552
Cdd:PRK15347 691 LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETT-QLWRDDPNNLDPdcMI 769
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 639298814 553 LAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALS 590
Cdd:PRK15347 770 VALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALE 807
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
223-590 4.61e-45

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 173.55  E-value: 4.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 223 KAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLD--QSDEALY 300
Cdd:PRK11466 436 EAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEagGKNVSVS 515
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 301 EEDVEFKTWLNNLCLLLSPLAEQKQLKfeLICNIPEQ--ACYYCDQQKLRQIIINLVGNAIKFTDHGTVKIQVDLVLEKQ 378
Cdd:PRK11466 516 DEPFEPRPLLESTLQLMSGRVKGRPIR--LATDIADDlpTALMGDPRRIRQVITNLLSNALRFTDEGSIVLRSRTDGEQW 593
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 379 LehtikISVKDSGPGIENDEIAYLTEPYVQSSAgkEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTVTFTLGE 458
Cdd:PRK11466 594 L-----VEVEDSGCGIDPAKLAEIFQPFVQVSG--KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVAT 666
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 459 LSLVEQRHQTKDyLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQ-AHHFDVVLLDMNLPDLTGQEVL 537
Cdd:PRK11466 667 APVPKTVNQAVR-LDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQnSEPFAAALVDFDLPDYDGITLA 745
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639298814 538 KRLKRIDHKNQRtpvLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALS 590
Cdd:PRK11466 746 RQLAQQYPSLVL---IGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLA 795
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
213-613 8.75e-42

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 164.14  E-value: 8.75e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  213 REQHLNKLADKAQkdleirglFLSTISHEIRTPLNGILGSAQLVmnQTSDTRNKAYCEAI---INSAESLNLLVDKVLDY 289
Cdd:PRK09959  702 RNKAINATVAKSQ--------FLATMSHEIRTPISSIMGFLELL--SGSGLSKEQRVEAIslaYATGQSLLGLIGEILDV 771
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  290 ASLDQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELICNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTVKI 369
Cdd:PRK09959  772 DKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAVKI 851
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  370 QVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFS 449
Cdd:PRK09959  852 TTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFT 931
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  450 FTVTF-TLGELSLVEQRHQTKDYL-TGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMN 527
Cdd:PRK09959  932 ITIPVeISQQVATVEAKAEQPITLpEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVN 1011
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  528 LPDLTGQEVLKRLKridHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALsdSQSNQTASIAVEL--- 604
Cdd:PRK09959 1012 MPNMDGFELTRKLR---EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHL--SQLHQVAHIAPQYrhl 1086
                         410
                  ....*....|
gi 639298814  605 -IDTLYDKTA 613
Cdd:PRK09959 1087 dIEALKNNTA 1096
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
220-603 5.12e-40

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 158.09  E-value: 5.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 220 LADK-AQKDLEIRGLFLSTISHEIRTPLNGILGSA-QLVMNQTSDTRnKAYCEAIINSAESLNLLVDKVLDYASLdqsdE 297
Cdd:PRK11107 281 LAKKrAQEAARIKSEFLANMSHELRTPLNGVIGFTrQTLKTPLTPTQ-RDYLQTIERSANNLLAIINDILDFSKL----E 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 298 A--LYEEDVEF--KTWLNNLCLLLSPLAEQKQLKFELIC--NIPEQACyyCDQQKLRQIIINLVGNAIKFTDHGTVKIQV 371
Cdd:PRK11107 356 AgkLVLENIPFslRETLDEVVTLLAHSAHEKGLELTLNIdpDVPDNVI--GDPLRLQQIITNLVGNAIKFTESGNIDILV 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 372 DLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ--SSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFS 449
Cdd:PRK11107 434 ELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQadASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFW 513
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 450 FTVTFTLGELSLVEQRHQtkDYLTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDgksaIELMQAHHFDVVLLDMNLP 529
Cdd:PRK11107 514 FHLPLDLNPNPIIDGLPT--DCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSPT----LSQLPEAHYDILLLGLPVT 587
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298814 530 DLTGQEVLK-RLKRIDHKNQRTpVLAFTaSLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSDSQSNQTASIAVE 603
Cdd:PRK11107 588 FREPLTMLHeRLAKAKSMTDFL-ILALP-CHEQVLAEQLKQDGADACLSKPLSHTRLLPALLEPCHHKQPPLLPP 660
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
347-454 1.12e-33

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


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 124.53  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVKIQVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ--SSAGKEKGGTGLGLAI 424
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQadSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 425 TSRLLEKLSSRLEIASQLGTGSVFSFTVTF 454
Cdd:cd16922   81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
211-449 8.38e-33

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 130.35  E-value: 8.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 211 ERREQHLNKLADkaqkdleIRGLfLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYA 290
Cdd:COG3852  123 ERELRRAEKLAA-------VGEL-AAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFS 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 291 SLDQSDealyEEDVEFKTWLNNLCLLLSP-LAEQKQLKFELICNIPEQacyYCDQQKLRQIIINLVGNAIK-FTDHGTVK 368
Cdd:COG3852  195 RPRPPE----REPVNLHEVLERVLELLRAeAPKNIRIVRDYDPSLPEV---LGDPDQLIQVLLNLVRNAAEaMPEGGTIT 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 369 IQV-----DLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVqssAGKEKgGTGLGLAITSRLLEKLSSRLEIASQLG 443
Cdd:COG3852  268 IRTrverqVTLGGLRPRLYVRIEVIDNGPGIPEEILDRIFEPFF---TTKEK-GTGLGLAIVQKIVEQHGGTIEVESEPG 343

                 ....*.
gi 639298814 444 TGSVFS 449
Cdd:COG3852  344 KGTTFR 349
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
234-451 1.38e-31

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 125.78  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  234 FLSTISHEIRTPLNGILGSAQLV--MNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEALYEEDVEFKTWLN 311
Cdd:TIGR02966 117 FVANVSHELRTPLTVLRGYLETLadGPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLD 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  312 NLCLLLSPLAEQKQLKFELIC--NIPEQAcyycDQQKLRQIIINLVGNAIKFTDHGTvKIQVDLVLEkqlEHTIKISVKD 389
Cdd:TIGR02966 197 HLRDEAEALSQGKNHQITFEIdgGVDVLG----DEDELRSAFSNLVSNAIKYTPEGG-TITVRWRRD---GGGAEFSVTD 268
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814  390 SGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:TIGR02966 269 TGIGIAPEHLPRLTERFyrVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
210-451 1.74e-31

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 129.13  E-value: 1.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 210 NERREQHLNKLAdKAQKDLEIrglFLSTISHEIRTPLNGILGSAQLVMNQTS---DTRNKAYCEAIINSAESLNLLVDKV 286
Cdd:COG4251  265 EEELEERTAELE-RSNEELEQ---FAYVASHDLREPLRKISGFSQLLEEDYGdklDEEGREYLERIRDAAERMQALIDDL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 287 LDYASLDQSDEALyeEDVEFKTWLNNLCLLLSPLAEQKQLKFElICNIPEqacYYCDQQKLRQIIINLVGNAIKFTDHGT 366
Cdd:COG4251  341 LAYSRVGRQELEF--EPVDLNELLEEVLEDLEPRIEERGAEIE-VGPLPT---VRGDPTLLRQVFQNLISNAIKYSRPGE 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 367 V-KIQVDLvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTG 445
Cdd:COG4251  415 PpRIEIGA---EREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEG 491

                 ....*.
gi 639298814 446 SVFSFT 451
Cdd:COG4251  492 ATFYFT 497
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
238-458 8.48e-30

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 122.76  E-value: 8.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 238 ISHEIRTPLNGILGSAQLVMNQTSDTRN------KAYCEAIINSAESLNLLVDKVLDYASLDQSDEalyeEDVEFKTWLN 311
Cdd:COG5000  208 IAHEIKNPLTPIQLSAERLRRKLADKLEedredlERALDTIIRQVDRLKRIVDEFLDFARLPEPQL----EPVDLNELLR 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 312 NLCLLLSPLAEQKQLKFELICNiPEQACYYCDQQKLRQIIINLVGNAIKFT-DHGTVKIQVdlvleKQLEHTIKISVKDS 390
Cdd:COG5000  284 EVLALYEPALKEKDIRLELDLD-PDLPEVLADRDQLEQVLINLLKNAIEAIeEGGEIEVST-----RREDGRVRIEVSDN 357
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 391 GPGIENDEIAYLTEPYVQSsagKEKGgTGLGLAITSRLLEKLSSRLEIASQLGTGSVfsFTVTFTLGE 458
Cdd:COG5000  358 GPGIPEEVLERIFEPFFTT---KPKG-TGLGLAIVKKIVEEHGGTIELESRPGGGTT--FTIRLPLAE 419
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
477-589 6.79e-29

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: 111.02  E-value: 6.79e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKNQRTPVLAFT 556
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
210-451 2.26e-28

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 117.21  E-value: 2.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 210 NERREQHLNKLAdKAQKdLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYC----EAIINSAESLNLLVDK 285
Cdd:COG4191  123 EEELRELQEQLV-QSEK-LAALGELAAGIAHEINNPLAAILGNAELLRRRLEDEPDPEELrealERILEGAERAAEIVRS 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 286 VLDYAslDQSDEALyeEDVEFKTWLNNLCLLLSPLAeqKQLKFELICNIPEQACY-YCDQQKLRQIIINLVGNAI---KF 361
Cdd:COG4191  201 LRAFS--RRDEEER--EPVDLNELIDEALELLRPRL--KARGIEVELDLPPDLPPvLGDPGQLEQVLLNLLINAIdamEE 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 362 TDHGTVKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSsagKEKG-GTGLGLAITSRLLEKLSSRLEIAS 440
Cdd:COG4191  275 GEGGRITIST-----RREGDYVVISVRDNGPGIPPEVLERIFEPFFTT---KPVGkGTGLGLSISYGIVEKHGGRIEVES 346
                        250
                 ....*....|.
gi 639298814 441 QLGTGSVFSFT 451
Cdd:COG4191  347 EPGGGTTFTIT 357
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
472-589 3.19e-28

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: 109.94  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 472 LTGLDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhKNQRTP 551
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALP-RLPDIP 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 639298814 552 VLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:COG0784   82 IIALTAYADEEDRERALEAGADDYLTKPVDPEELLEAL 119
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
212-590 1.73e-27

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 118.92  E-value: 1.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 212 RREQHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYAS 291
Cdd:PRK10841 428 KMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSK 507
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 292 LDQsdEALYEEDVEF--KTWLNNLCLLLSPLAEQKQLkfELIC----NIPEQACyyCDQQKLRQIIINLVGNAIKFTDHG 365
Cdd:PRK10841 508 IES--EQLKIEPREFspREVINHITANYLPLVVKKRL--GLYCfiepDVPVALN--GDPMRLQQVISNLLSNAIKFTDTG 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 366 TVKIQVdLVLEKQLEhtikISVKDSGPGIENDEIAYLTEPYVQSSAGKEKG--GTGLGLAITSRLLEKLSSRLEIASQLG 443
Cdd:PRK10841 582 CIVLHV-RVDGDYLS----FRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNfqGTGLGLAICEKLINMMDGDISVDSEPG 656
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 444 TGSVFS---------FTVTFTLGELS--------------------LVEQRHQTKDY----LTGLDVLLVED---LDLNQ 487
Cdd:PRK10841 657 MGSQFTiriplygaqYPQKKGVEGLQgkrcwlavrnasleqfletlLQRSGIQVQRYegqePTPEDVLITDDpvqKKWQG 736
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 488 KIAIEFMAD--------------------------------------------------------------DEHKI---- 501
Cdd:PRK10841 737 RAVITFCRRhigipleiapgewvhstatphelpallariyrielesddsanalpstdkavsdnddmmilvvDDHPInrrl 816
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 502 ------------KLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFTASLSPDEVKEYLE 569
Cdd:PRK10841 817 ladqlgslgyqcKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQ---LGLTLPVIGVTANALAEEKQRCLE 893
                        490       500
                 ....*....|....*....|.
gi 639298814 570 LGIKDIVGKPIKHEKLRQALS 590
Cdd:PRK10841 894 AGMDSCLSKPVTLDVLKQTLT 914
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
211-451 4.39e-27

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: 115.46  E-value: 4.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 211 ERREqhLNKLADKAQKdLEIRGLFLSTISHEIRTPLNGILGSAQLvMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYA 290
Cdd:COG5809  253 ERKK--LEELLRKSEK-LSVVGELAAGIAHEIRNPLTSLKGFIQL-LKDTIDEEQKTYLDIMLSELDRIESIISEFLVLA 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 291 SldqsDEALYEEDVEFKTWLNNLCLLLSPLAEQK--QLKFELICNIPeqaCYYCDQQKLRQIIINLVGNAIKFT-DHGTV 367
Cdd:COG5809  329 K----PQAIKYEPKDLNTLIEEVIPLLQPQALLKnvQIELELEDDIP---DILGDENQLKQVFINLLKNAIEAMpEGGNI 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 368 KIQVDLVLEKQlehtIKISVKDSGPGIENDEIAYLTEPYvqsSAGKEKgGTGLGLAITSRLLEKLSSRLEIASQLGTGSV 447
Cdd:COG5809  402 TIETKAEDDDK----VVISVTDEGCGIPEERLKKLGEPF---YTTKEK-GTGLGLMVSYKIIEEHGGKITVESEVGKGTT 473

                 ....
gi 639298814 448 FSFT 451
Cdd:COG5809  474 FSIT 477
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
215-451 4.54e-25

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 108.56  E-value: 4.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 215 QHLNKLADKAQ-KDLE-IRGLFLSTISHEIRTPLNGILGSAQLVMNQTSD--TRNKAYcEAIINSAESLNLLVDKVLDYA 290
Cdd:PRK11006 186 QLLMVARDVTQmHQLEgARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEgaLREKAL-HTMREQTQRMEGLVKQLLTLS 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 291 SLDQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQlkfELICNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTvKIQ 370
Cdd:PRK11006 265 KIEAAPTIDLNEKVDVPMMLRVLEREAQTLSQGKH---TITFEVDNSLKVFGNEDQLRSAISNLVYNAVNHTPEGT-HIT 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 371 VDLvleKQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVF 448
Cdd:PRK11006 341 VRW---QRVPQGAEFSVEDNGPGIAPEHIPRLTERFyrVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRF 417

                 ...
gi 639298814 449 SFT 451
Cdd:PRK11006 418 SFV 420
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
343-452 4.54e-25

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 100.03  E-value: 4.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814   343 DQQKLRQIIINLVGNAIKFT-DHGTVKIQVDLVlekqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEK-GGTGL 420
Cdd:smart00387   2 DPDRLRQVLSNLLDNAIKYTpEGGRITVTLERD-----GDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKiGGTGL 76
                           90       100       110
                   ....*....|....*....|....*....|..
gi 639298814   421 GLAITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:smart00387  77 GLSIVKKLVELHGGEISVESEPGGGTTFTITL 108
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
347-451 1.53e-24

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 98.44  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTvKIQVDLvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITS 426
Cdd:cd00075    1 LEQVLSNLLDNALKYSPPGG-TIEISL---RQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGLGLAIVR 76
                         90       100
                 ....*....|....*....|....*
gi 639298814 427 RLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:cd00075   77 RIVEAHGGRITVESEPGGGTTFTVT 101
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
477-589 3.60e-24

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: 99.98  E-value: 3.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFT 556
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRA-DPRTADIPIIFLT 82
                         90       100       110
                 ....*....|....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:COG3706   83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
36-454 2.05e-23

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 103.41  E-value: 2.05e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  36 LLYIFYPILLLGSVIGFTLVG-DTHNLVIISAassmMFAASIVHCLSLS-QFLN----------------YRGIGFKLLC 97
Cdd:COG5806    8 LLFILLPIFIYQIFWEDRRRNkPVKNRMLIGV----LSSIAIILCMTFPiHITDgfifdlrqvpiilgtlYGGWRVGLFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  98 SVtafctVMLGYYTFFDPslhERVIASDIQHIAEAGFLLFI---FIKCARKpypnGSIVYITILTLV-ALSFIGRSLFMD 173
Cdd:COG5806   84 FL-----ILLLYRFYLGG---EGVFVTLLVYTVILILPLLLrrkFHRLSRK----GKIVLAILLSFLsALLLLLLAIIFI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 174 NIEQKNLLVNGWFssllflnGVIAPMFYAAGMALLCNERREQHLNKLADKAQKdLEIRGLFLSTISHEIRTPLNGILGSA 253
Cdd:COG5806  152 ADISELLDFILYF-------IIIQLLAMLIAVYLIENLIENILLRKELQRAEK-LEVVSELAASIAHEVRNPLTVVRGFI 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 254 QLVM-NQTSDTRNKAY----------CEAIINsaeslnllvdkvlDYASLDQSDEALYEEdVEFKTWLNNLCLLLSPLAE 322
Cdd:COG5806  224 QLLQePELSDEKRKQYirialeeldrAEAIIT-------------DYLTFAKPQPEKLEK-IDVSEELEHVIDVLSPYAN 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 323 QKqlKFELICNIPEQACYYCDQQKLRQIIINLVGNAIK-FTDHGTVKIQVDLVlekqlEHTIKISVKDSGPGIENDEIAY 401
Cdd:COG5806  290 MN--NVEIQTELEPGLYIEGDRQKLQQCLINIIKNGIEaMPNGGTLTIDVSID-----KNKVIISIKDTGVGMTKEQLER 362
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639298814 402 LTEPYVQSsagKEKgGTGLGLAITSRLLEKLSSRLEIASQLGTGSvfSFTVTF 454
Cdd:COG5806  363 LGEPYFST---KEK-GTGLGTMVSYRIIEAMNGTIRVESEVGKGT--TFTITL 409
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
477-589 3.04e-22

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 92.21  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFT 556
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPT---TPVIILT 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 639298814  557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:pfam00072  78 AHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
477-590 3.05e-22

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 96.00  E-value: 3.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFT 556
Cdd:COG3437    9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRA-DPSTRDIPVIFLT 87
                         90       100       110
                 ....*....|....*....|....*....|....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALS 590
Cdd:COG3437   88 ALADPEDRERALEAGADDYLTKPFDPEELLARVR 121
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
343-452 3.38e-22

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: 92.05  E-value: 3.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  343 DQQKLRQIIINLVGNAIKFTDHGTvKIQVDLVLEKQLEhtikISVKDSGPGIENDEIAYLTEPYVQSSAGKEkGGTGLGL 422
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAAKAG-EITVTLSEGGELT----LTVEDNGIGIPPEDLPRIFEPFSTADKRGG-GGTGLGL 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 639298814  423 AITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:pfam02518  76 SIVRKLVELLGGTITVESEPGGGTTVTLTL 105
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
472-590 8.91e-22

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 91.57  E-value: 8.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 472 LTGLDVLLVEDLDLNQKIAIEFMADDE--HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQR 549
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRA---RGPD 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 639298814 550 TPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALS 590
Cdd:COG4565   78 VDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALE 118
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
228-454 1.58e-21

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: 98.65  E-value: 1.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 228 LEIRGLFLSTISHEIRTPLNGILGSAQLVmnQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASldqsDEALYEEDVEFK 307
Cdd:COG5805  284 LSIAGQLAAGIAHEIRNPLTSIKGFLQLL--QPGIEDKEEYFDIMLSELDRIESIISEFLALAK----PQAVNKEKENIN 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 308 TWLNNLCLLLSPLAEQKQLKFELIcNIPEQACYYCDQQKLRQIIINLVGNAIK-FTDHGTVKIQVdlvleKQLEHTIKIS 386
Cdd:COG5805  358 ELIQDVVTLLETEAILHNIQIRLE-LLDEDPFIYCDENQIKQVFINLIKNAIEaMPNGGTITIHT-----EEEDNSVIIR 431
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 387 VKDSGPGIENDEIAYLTEPYVQSsagKEKGgTGLGLAITSRLLEKLSSRLEIASQLGTGSVfsFTVTF 454
Cdd:COG5805  432 VIDEGIGIPEERLKKLGEPFFTT---KEKG-TGLGLMVSYKIIENHNGTIDIDSKVGKGTT--FTITL 493
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
477-605 1.06e-20

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: 95.42  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHknqRTPVLAFT 556
Cdd:COG2204    5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDP---DLPVILLT 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL----RQALSDSQSNQTASIAVELI 605
Cdd:COG2204   82 GYGDVETAVEAIKAGAFDYLTKPFDLEELlaavERALERRRLRRENAEDSGLI 134
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-450 2.85e-20

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: 86.49  E-value: 2.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFT---DHGTVKIQvdlvlekQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLG 421
Cdd:cd16952    1 LRSAFSNLVSNAVKYTppsDTITVRWS-------QEESGARLSVEDTGPGIPPEHIPRLTERFyrVDIERCRNTGGTGLG 73
                         90       100
                 ....*....|....*....|....*....
gi 639298814 422 LAITSRLLEKLSSRLEIASQLGTGSVFSF 450
Cdd:cd16952   74 LAIVKHVMSRHDARLLIASELGKGSRFTC 102
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
215-454 3.35e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 94.12  E-value: 3.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 215 QHLNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVmnqtSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQ 294
Cdd:NF012163 224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAI----QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSM 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 295 SDE-ALyeedVEFKTWLNNLCLLLSPLA------EQKQLKFELicNIPEQACYYCDQQKLRQIIINLVGNAIKFTDH-GT 366
Cdd:NF012163 300 SDEgAL----AYQKASVDLVPLLEVEGGafrerfASAGLELEV--SLPDSSLVFGDRDRLMQLFNNLLENSLRYTDSgGS 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 367 VKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIA-SQLG 443
Cdd:NF012163 374 LHISA-----SQRPKEVTLTVADSAPGVSDEQLARLFERFyrVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAhSPLG 448
                        250
                 ....*....|.
gi 639298814 444 TGSVfsfTVTF 454
Cdd:NF012163 449 GLRI---VVTL 456
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
477-589 1.35e-19

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: 87.70  E-value: 1.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:COG0745    4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA---RPSDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARI 113
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
478-579 2.43e-19

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


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 83.43  E-value: 2.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 478 LLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFTA 557
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPD---IPVIVLTA 77
                         90       100
                 ....*....|....*....|..
gi 639298814 558 SLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd00156   78 KADEEDAVRALELGADDYLVKP 99
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
225-450 3.92e-18

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 88.49  E-value: 3.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 225 QKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSdealYEEDV 304
Cdd:PRK11360 384 QERLAALGELVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRES----QWQPV 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 305 EFKTWLNNLCLLLSPLAEQKQLKFELIC--NIPEqacYYCDQQKLRQIIINLVGNAIK-FTDHGTVKIQVDLVLEKQLEh 381
Cdd:PRK11360 460 SLNALVEEVLQLFQTAGVQARVDFETELdnELPP---IWADPELLKQVLLNILINAVQaISARGKIRIRTWQYSDGQVA- 535
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 382 tikISVKDSGPGIENDEIAYLTEPYVQSSAgkekGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSF 450
Cdd:PRK11360 536 ---VSIEDNGCGIDPELLKKIFDPFFTTKA----KGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
477-591 1.21e-17

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: 79.16  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlNQKIAI---EFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVlkrLKRIDHKNQRTPVL 553
Cdd:cd17572    1 VLLVED---SPSLAAlyqEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEI---LKWIQERSLPTSVI 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSD 591
Cdd:cd17572   75 VITAHGSVDIAVEAMRLGAYDFLEKPFDADRLRVTVRN 112
PRK09303 PRK09303
histidine kinase;
235-452 2.27e-17

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 84.62  E-value: 2.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 235 LSTISHEIRTPLNGI---LGSAQLVMNQTSDTRNKAYCEAIINSA----ESLNLLVDKVLDYASldQSDEALYEEDVefK 307
Cdd:PRK09303 155 LAMLAHDLRTPLTAAslaLETLELGQIDEDTELKPALIEQLQDQArrqlEEIERLITDLLEVGR--TRWEALRFNPQ--K 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 308 TWLNNLC----LLLSPLAEQKQLKFELicNIPEQ-ACYYCDQQKLRQIIINLVGNAIKFT-DHGTVKIQVdlvlekqLEH 381
Cdd:PRK09303 231 LDLGSLCqeviLELEKRWLAKSLEIQT--DIPSDlPSVYADQERIRQVLLNLLDNAIKYTpEGGTITLSM-------LHR 301
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298814 382 T---IKISVKDSGPGIENDEIAYLTEPYV--QSSAGKEkgGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:PRK09303 302 TtqkVQVSICDTGPGIPEEEQERIFEDRVrlPRDEGTE--GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTL 375
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
234-443 1.27e-16

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: 83.21  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  234 FLSTISHEIRTPLNGILGSAQLVMNQTSDtrNKAYCEAIINSAESLNLL---VDKVLDYASLDQSDEALYEEDVEFKTWL 310
Cdd:TIGR01386 244 FSADLAHELRTPLTNLLGQTQVALSQPRT--GEEYREVLESNLEELERLsrmVSDMLFLARADNGQLALERVRLDLAAEL 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  311 NNLCLLLSPLAEQK--QLKFELICNIPeqacyyCDQQKLRQIIINLVGNAIKFTDHGTvkiQVDLVLEKQLEHTiKISVK 388
Cdd:TIGR01386 322 AKVAEYFEPLAEERgvRIRVEGEGLVR------GDPQMFRRAISNLLSNALRHTPDGG---TITVRIERRSDEV-RVSVS 391
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 639298814  389 DSGPGIENDEIAYLTEP-YVQSSAGKEKG-GTGLGLAITSRLLEKLSSRLEIASQLG 443
Cdd:TIGR01386 392 NPGPGIPPEHLSRLFDRfYRVDPARSNSGeGTGLGLAIVRSIMEAHGGRASAESPDG 448
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
211-448 1.58e-16

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 83.96  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 211 ERREQHlnkladkAQKdLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQT-SDTRNKAYCEAIINSAESLNLLVDKVLDY 289
Cdd:PRK13837 438 ERRLEH-------ARR-LEAVGTLASGIAHNFNNILGAILGYAEMALNKLaRHSRAARYIDEIISAGARARLIIDQILAF 509
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 290 ASLDQS-------DEALYEedvefktwlnNLCLLLSPLAEQKQLKFELIcniPEQACYYCDQQKLRQIIINLVGNAIK-F 361
Cdd:PRK13837 510 GRKGERntkpfdlSELVTE----------IAPLLRVSLPPGVELDFDQD---QEPAVVEGNPAELQQVLMNLCSNAAQaM 576
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 362 TDHGTVKIQVD---LVLEKQLEHT-------IKISVKDSGPGIENDEIAYLTEPYVQSSAGkekgGTGLGLAITSRLLEK 431
Cdd:PRK13837 577 DGAGRVDISLSrakLRAPKVLSHGvlppgryVLLRVSDTGAGIDEAVLPHIFEPFFTTRAG----GTGLGLATVHGIVSA 652
                        250
                 ....*....|....*..
gi 639298814 432 LSSRLEIASQLGTGSVF 448
Cdd:PRK13837 653 HAGYIDVQSTVGRGTRF 669
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
477-580 1.93e-16

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 75.24  E-value: 1.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKrIDHKNQRTPVLAFT 556
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLK-ADPATRHIPVIFLT 79
                         90       100
                 ....*....|....*....|....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPI 580
Cdd:cd19920   80 ALTDTEDKVKGFELGAVDYITKPF 103
envZ PRK09467
osmolarity sensor protein; Provisional
231-437 5.46e-16

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 81.11  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 231 RGLFLSTISHEIRTPLNGI-LGSAqlVMNQTSDtrnkaYC-EAIINSAESLNLLVDKVLDYASLDQsdealyEEDVEFkT 308
Cdd:PRK09467 229 RTLLMAGVSHDLRTPLTRIrLATE--MMSEEDG-----YLaESINKDIEECNAIIEQFIDYLRTGQ------EMPMEM-A 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 309 WLNNLC--LLLSPLAEQKQLKFEL---ICNIPEQACyycdqqKLRQIIINLVGNAIKFTdHGTVKIqvdlvLEKQLEHTI 383
Cdd:PRK09467 295 DLNALLgeVIAAESGYEREIETALqpgPIEVPMNPI------AIKRALANLVVNAARYG-NGWIKV-----SSGTEGKRA 362
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 384 KISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITSRLLE------KLSSRLE 437
Cdd:PRK09467 363 WFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSGTGLGLAIVKRIVDqhngkvELGNSEE 422
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
343-454 3.20e-15

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: 72.11  E-value: 3.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFTDH-GTVKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTG 419
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTgGKLRIRA-----AQTPQEVRLDVEDSAPGVSDDQLARLFERFyrVESSRNRASGGSG 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 639298814 420 LGLAITSRLLEKLSSRLEIA-SQLGTgsvFSFTVTF 454
Cdd:cd16946   76 LGLAICHNIALAHGGTISAEhSPLGG---LRLVLTL 108
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
237-456 3.62e-15

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 78.73  E-value: 3.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 237 TISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEALYEEDVEFKTWLNNLCLL 316
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEA 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 317 LSPLAEQKQLKFELicnIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTVkiqVDLVLEKQlEHTIKISVKDSGPGIEN 396
Cdd:PRK11100 342 REAQAAAKGITLRL---RPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGT---ITLSAEVD-GEQVALSVEDQGPGIPD 414
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 639298814 397 DEIAYLTEPY--VQSSAGKEKgGTGLGLAITSRLLEKLSSRLEIASQLGTGSVfsftVTFTL 456
Cdd:PRK11100 415 YALPRIFERFysLPRPANGRK-STGLGLAFVREVARLHGGEVTLRNRPEGGVL----ATLTL 471
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
207-479 4.28e-15

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 79.21  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 207 LLCNERREQHLNKLADKAQ----KDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLL 282
Cdd:PRK10618 422 LLRDQDREVLVNKKLQQAQreyeKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRL 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 283 VDKVLDYASLDQSDEALYEEDVEFKTWLNNLCLLLSPLAEQKQLKFELICNIPEQACYYCDQQKLRQIIINLVGNAIKFT 362
Cdd:PRK10618 502 VDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTT 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 363 DHGtvKIQVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYV-QSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQ 441
Cdd:PRK10618 582 AYG--KITLEVDQDESSPDRLTIRILDTGAGVSIKELDNLHFPFLnQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSR 659
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 639298814 442 LGTGSVFSFTVTFTLGELslvEQRHQTKDYLTGLDVLL 479
Cdd:PRK10618 660 EGLGTRYSIHLKMLAADP---EVEEEEEKLLDGVTVLL 694
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
477-579 5.18e-15

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 71.34  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDE--HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLA 554
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPD---TKIII 78
                         90       100
                 ....*....|....*....|....*
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:COG4753   79 LSGYSDFEYAQEAIKLGADDYLLKP 103
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
493-591 6.22e-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: 71.41  E-value: 6.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 493 FMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFTASLSPDEVKEYLELGI 572
Cdd:cd17593   20 LPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLE---TKVIVVSGDVQPEAKERVLELGA 96
                         90
                 ....*....|....*....
gi 639298814 573 KDIVGKPIKHEKLRQALSD 591
Cdd:cd17593   97 LAFLKKPFDPEKLAQLLEE 115
PRK10604 PRK10604
sensor protein RstB; Provisional
218-450 9.78e-15

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.95  E-value: 9.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 218 NKLADKAQKDLEIRGLFLSTISHEIRTPLNGIlgSAQLVMnqtSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDE 297
Cdd:PRK10604 199 NQMADNINALIASKKQLIDGIAHELRTPLVRL--RYRLEM---SDNLSAAESQALNRDIGQLEALIEELLTYARLDRPQN 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 298 ALYEEDVEFKTWLNnlclllSPLAEQKQL--KFELICNIPEQACY-YCDQQKLRQIIINLVGNAIKFTdHGTVkiQVDLV 374
Cdd:PRK10604 274 ELHLSEPDLPAWLS------THLADIQAVtpEKTVRLDTPHQGDYgALDMRLMERVLDNLLNNALRYA-HSRV--RVSLL 344
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 375 LEKQlehTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEK--GGTGLGLAITSRLLEKLSSRLEI-ASQLGtGSVFSF 450
Cdd:PRK10604 345 LDGN---QACLIVEDDGPGIPPEERERVFEPFVRLDPSRDRatGGCGLGLAIVHSIALAMGGSVNCdESELG-GARFSF 419
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
215-430 1.46e-14

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 76.60  E-value: 1.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 215 QHLNKLADKAQKDLEIRGLFLSTISHEIRTPL---NGILGSAQ-LVMNQTSDTrnkayceaiINS--AESLNL--LVDkv 286
Cdd:PRK10549 224 QDFNQLASTLEKNEQMRRDFMADISHELRTPLavlRGELEAIQdGVRKFTPES---------VASlqAEVGTLtkLVD-- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 287 lDYASLDQSDE-AL-YEedvefKTWLNNLCLLLSPLA------EQKQLKFELicNIPEQACYYCDQQKLRQIIINLVGNA 358
Cdd:PRK10549 293 -DLHQLSLSDEgALaYR-----KTPVDLVPLLEVAGGafrerfASRGLTLQL--SLPDSATVFGDPDRLMQLFNNLLENS 364
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298814 359 IKFTD-HGTVKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAITSRLLE 430
Cdd:PRK10549 365 LRYTDsGGSLHISA-----EQRDKTLRLTFADSAPGVSDEQLQKLFERFyrTEGSRNRASGGSGLGLAICLNIVE 434
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
477-586 1.50e-14

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: 70.55  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIaIEFMA--DDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHkNQRTPVLA 554
Cdd:cd17551    3 ILIVDDNPTNLLL-LEALLrsAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPG-LEDVPIVM 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKLR 586
Cdd:cd17551   81 ITADTDREVRLRALEAGATDFLTKPFDPVELL 112
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
189-448 2.88e-14

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 75.59  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 189 LLFLNGVIAPMFYAAGMALLCNERREQHLNKLAD--KAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLVMNQT-SDTRN 265
Cdd:PRK10364 193 TLIILFALATVLLASLLAFFWYRRYLRSRQLLQDemKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERApAGGEA 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 266 KAYCEAIINSAESLNLLVDKVLDYASldQSDEALyeEDVEFKTWLNNLCLLLSPLAEQK--QLKFELICNIPE-QAcyyc 342
Cdd:PRK10364 273 HQLAQVMAKEADRLNRVVSELLELVK--PTHLAL--QAVDLNDLINHSLQLVSQDANSReiQLRFTANDTLPEiQA---- 344
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFTD-HGTVKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGkekgGTGLG 421
Cdd:PRK10364 345 DPDRLTQVLLNLYLNAIQAIGqHGVISVTA-----SESGAGVKISVTDSGKGIAADQLEAIFTPYFTTKAE----GTGLG 415
                        250       260
                 ....*....|....*....|....*..
gi 639298814 422 LAITSRLLEKLSSRLEIASQLGTGSVF 448
Cdd:PRK10364 416 LAVVHNIVEQHGGTIQVASQEGKGATF 442
glnL PRK11073
nitrogen regulation protein NR(II);
205-440 4.24e-14

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 74.35  E-value: 4.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 205 MALLCNERR-EQHLNKLADK-AQKDLeIRGLflstiSHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLL 282
Cdd:PRK11073 108 MAPMDNQRRlSQEQLQHAQQvAARDL-VRGL-----AHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNL 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 283 VDKVLD--------YASLDQSDEALYeedvefktwlnNLCLLLSPlaEQKQLKFELICNIPEqacYYCDQQKLRQIIINL 354
Cdd:PRK11073 182 VDRLLGpqrpgthvTESIHKVAERVV-----------QLVSLELP--DNVRLIRDYDPSLPE---LAHDPDQIEQVLLNI 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 355 VGNAIKF--TDHGTVKIQVDLVLEKQLEHT-----IKISVKDSGPGIE---NDEIAYltePYVqssAGKEkGGTGLGLAI 424
Cdd:PRK11073 246 VRNALQAlgPEGGTITLRTRTAFQLTLHGEryrlaARIDIEDNGPGIPphlQDTLFY---PMV---SGRE-GGTGLGLSI 318
                        250
                 ....*....|....*.
gi 639298814 425 TSRLLEKLSSRLEIAS 440
Cdd:PRK11073 319 ARNLIDQHSGKIEFTS 334
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
478-579 5.61e-14

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: 68.20  E-value: 5.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 478 LLVEDldlNQKIA---IEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLA 554
Cdd:cd17574    1 LVVED---DEEIAellSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE---KGSDIPIIM 74
                         90       100
                 ....*....|....*....|....*
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17574   75 LTAKDEEEDKVLGLELGADDYITKP 99
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-452 5.68e-14

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 68.19  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVKI-QVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSsagkEKGGTGLGLAIT 425
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGGCERrELTIRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTT----KSEGLGMGLSIC 76
                         90       100
                 ....*....|....*....|....*..
gi 639298814 426 SRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:cd16920   77 RSIIEAHGGRLSVESPAGGGATFQFTL 103
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
504-589 6.51e-14

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 68.69  E-value: 6.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHknqRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHE 583
Cdd:cd17535   30 AADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYP---DLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPE 106

                 ....*.
gi 639298814 584 KLRQAL 589
Cdd:cd17535  107 ELIEAI 112
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-445 9.70e-14

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: 67.47  E-value: 9.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDhGTVKIQVDLVLEKqlehtIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITS 426
Cdd:cd16950    1 LKRVLSNLVDNALRYGG-GWVEVSSDGEGNR-----TRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGLAIVQ 74
                         90
                 ....*....|....*....
gi 639298814 427 RLLEKLSSRLEIASQLGTG 445
Cdd:cd16950   75 RISDAHGGSLTLANRAGGG 93
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
231-294 1.83e-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: 65.70  E-value: 1.83e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814  231 RGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQ 294
Cdd:pfam00512   2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEA 65
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
476-589 2.41e-13

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: 67.44  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 476 DVLLVEDLDLNQKIAIEFM--ADDEHKIKLAKDGKSAIELM-------QAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHK 546
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFkeAGVPNELHVVRDGEEALDFLrgegeyaDAPRPDLILLDLNMPRMDGFEVLREIKA-DPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 639298814 547 NQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17557   80 LRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAI 122
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
474-589 4.54e-13

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 68.44  E-value: 4.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 474 GLDVLLVEDLDLNQKIAIEFMADDEHK-IKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhkNQRTPV 552
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE----ERPAPV 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 639298814 553 LAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:COG3707   79 ILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-445 6.58e-13

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 65.50  E-value: 6.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTvkiQVDLVLEKqlEHTIKISVKDSGPGIENDEIAYLTEPYVQsSAGKEKGGTGLGLAITS 426
Cdd:cd16940   14 LFLLLRNLVDNAVRYSPQGS---RVEIKLSA--DDGAVIRVEDNGPGIDEEELEALFERFYR-SDGQNYGGSGLGLSIVK 87
                         90
                 ....*....|....*....
gi 639298814 427 RLLEKLSSRLEIASQLGTG 445
Cdd:cd16940   88 RIVELHGGQIFLGNAQGGG 106
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
475-591 6.98e-13

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: 65.73  E-value: 6.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDldlnqkiaiEFMADDEHK-----------IKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRi 543
Cdd:cd19925    1 INVLIVED---------DPMVAEIHRayveqvpgftvIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRA- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 639298814 544 dhKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSD 591
Cdd:cd19925   71 --AGHDVDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLER 116
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-451 1.35e-12

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: 64.27  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVKiQVDLVLEKQ-LEHTIkiSVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAIT 425
Cdd:cd16921    1 LGQVLTNLLGNAIKFRRPRRPP-RIEVGAEDVgEEWTF--YVRDNGIGIDPEYAEKVFGIFQRLHSREEYEGTGVGLAIV 77
                         90       100
                 ....*....|....*....|....*.
gi 639298814 426 SRLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:cd16921   78 RKIIERHGGRIWLESEPGEGTTFYFT 103
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
477-585 1.54e-12

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: 64.43  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:cd17624    1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRR---QGQSLPVLILT 77
                         90       100
                 ....*....|....*....|....*....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17624   78 ARDGVDDRVAGLDAGADDYLVKPFALEEL 106
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
231-294 1.59e-12

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 62.97  E-value: 1.59e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814   231 RGLFLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQ 294
Cdd:smart00388   2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEA 65
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
477-585 2.06e-12

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: 64.23  E-value: 2.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAF 555
Cdd:cd19934    1 LLLVEDdALLAAQLK-EQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA---TPVLIL 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd19934   77 TARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
477-580 2.75e-12

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: 63.71  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFT 556
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKE-DPATRDIPVIALT 80
                         90       100
                 ....*....|....*....|....*
gi 639298814 557 A-SLSPDEVKeYLELGIKDIVGKPI 580
Cdd:cd17548   81 AyAMKGDREK-ILEAGCDGYISKPI 104
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
228-290 4.43e-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: 61.46  E-value: 4.43e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814 228 LEIRGLFLSTISHEIRTPLNGILGSAQ-LVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYA 290
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALElLEEELLDDEEQREYLERIREEAERLLRLINDLLDLS 64
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
343-446 6.54e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 62.55  E-value: 6.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFTD-HGTVKIQVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAgkekGGTGLG 421
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEgRPSDVGEVRIRVEADQDGRIVLIVCDNGKGFPREMRHRATEPYVTTRP----KGTGLG 76
                         90       100
                 ....*....|....*....|....*
gi 639298814 422 LAITSRLLEKLSSRLEIASQLGTGS 446
Cdd:cd16944   77 LAIVKKIMEEHGGRISLSNREAGGA 101
PRK10490 PRK10490
sensor protein KdpD; Provisional
216-451 1.01e-11

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 68.52  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 216 HLNKLADKAQKDLE---IRGLFLSTISHEIRTPLNGILGSAQLVM-----------NQTSDTRnkaycEAIINSAEslnl 281
Cdd:PRK10490 646 TLTASEEQARLASEreqLRNALLAALSHDLRTPLTVLFGQAEILTldlasegsphaRQASEIR-----QQVLNTTR---- 716
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 282 LVDKVLDYASLDQSDEALYEEdvefktWL-------NNLCLLLSPLAEQkqlkfELICNIPEQ-ACYYCDQQKLRQIIIN 353
Cdd:PRK10490 717 LVNNLLDMARIQSGGFNLRKE------WLtleevvgSALQMLEPGLSGH-----PINLSLPEPlTLIHVDGPLFERVLIN 785
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 354 LVGNAIKFTDHGTvKIQVDLVLEKQlehTIKISVKDSGPGIENDEIAYLTEPYvqSSAGKEKG--GTGLGLAITSRLLEK 431
Cdd:PRK10490 786 LLENAVKYAGAQA-EIGIDAHVEGE---RLQLDVWDNGPGIPPGQEQLIFDKF--ARGNKESAipGVGLGLAICRAIVEV 859
                        250       260
                 ....*....|....*....|
gi 639298814 432 LSSRLEIASQLGTGSVFSFT 451
Cdd:PRK10490 860 HGGTIWAENRPEGGACFRVT 879
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-448 2.76e-11

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: 60.90  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTD-HGTVKIQVDLVLEKQlehtiKISVKDSGPGIENDEIAYLTEPYVQSSAGKEkgGTGLGLAIT 425
Cdd:cd16943    4 LNQVLLNLLVNAAQAMEgRGRITIRTWAHVDQV-----LIEVEDTGSGIDPEILGRIFDPFFTTKPVGE--GTGLGLSLS 76
                         90       100
                 ....*....|....*....|...
gi 639298814 426 SRLLEKLSSRLEIASQLGTGSVF 448
Cdd:cd16943   77 YRIIQKHGGTIRVASVPGGGTRF 99
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
504-591 2.93e-11

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 61.14  E-value: 2.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhKNQRtpVLAFTASLSPDEVKEYLELGIKDIVGKPIKHE 583
Cdd:cd17542   31 AANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKID-PNAK--VIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPE 107

                 ....*...
gi 639298814 584 KLRQALSD 591
Cdd:cd17542  108 RVLEAVEK 115
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
477-589 4.78e-11

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: 60.16  E-value: 4.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlNQKIA--IEFMADDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHkNQRTPVL 553
Cdd:cd17580    1 ILVVDD---NEDAAemLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPW-LANTPAI 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17580   77 ALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
343-448 5.11e-11

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 60.20  E-value: 5.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFT-DHGTVKIqvdlVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQ--SSAGKEKGGTG 419
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTpDGGRIRC----ILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQgdGSSTRAHGGTG 76
                         90       100
                 ....*....|....*....|....*....
gi 639298814 420 LGLAITSRLLEKLSSRLEIASQLGTGSVF 448
Cdd:cd16925   77 LGLSIVKEFVELHGGTVTVSDAPGGGALF 105
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
477-579 5.66e-11

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 59.76  E-value: 5.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlNQKIAiEFMA----DDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPV 552
Cdd:cd19935    1 ILVVED---EKKLA-EYLKkgltEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRA---AGKQTPV 73
                         90       100
                 ....*....|....*....|....*..
gi 639298814 553 LAFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd19935   74 LMLTARDSVEDRVKGLDLGADDYLVKP 100
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
477-580 7.70e-11

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: 59.43  E-value: 7.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFT 556
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKE-DPETRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....*
gi 639298814 557 AsLSPDEVK-EYLELGIKDIVGKPI 580
Cdd:cd17538   81 A-LDDREDRiRGLEAGADDFLSKPI 104
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
477-589 1.02e-10

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: 59.66  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlnQKIAIEFMAD----DEHKIKL---AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhkNQR 549
Cdd:cd17536    1 VLIVDD----EPLIREGLKKlidwEELGFEVvgeAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIREL---YPD 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 639298814 550 TPVLAFTASlspDE---VKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17536   74 IKIIILSGY---DDfeyAQKAIRLGVVDYLLKPVDEEELEEAL 113
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
478-579 1.05e-10

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: 59.16  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 478 LLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:cd17625    1 LVVEDeKDLSEAIT-KHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLRE---EGIETPVLLLT 76
                         90       100
                 ....*....|....*....|....
gi 639298814 557 A-SLSPDEVKEyLELGIKDIVGKP 579
Cdd:cd17625   77 AlDAVEDRVKG-LDLGADDYLPKP 99
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
477-608 1.12e-10

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 59.71  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKI---AIEfmADDEHK-IKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhknQRTPV 552
Cdd:cd17541    3 VLIVDDSAVMRKLlsrILE--SDPDIEvVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE----RPTPV 76
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 553 LAFTASLSP--DEVKEYLELGIKDIVGKPikheklrqalSDSQSNQTASIAVELIDTL 608
Cdd:cd17541   77 VMVSSLTEEgaEITLEALELGAVDFIAKP----------SGGISLDLEEIAEELIEKI 124
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
343-451 1.18e-10

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


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 58.84  E-value: 1.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFTDHGTvKIQVDLvleKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAG-KEKGGTGLG 421
Cdd:cd16948    2 DAKWLSFIIGQIVSNALKYSKQGG-KIEIYS---ETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENGrNFQESTGMG 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 422 LAITSRLLEKLSSRLEIASQLGTGSVFSFT 451
Cdd:cd16948   78 LYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
504-589 1.19e-10

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 59.27  E-value: 1.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLkRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHE 583
Cdd:cd19923   31 AEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTI-RADGALSHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAA 109

                 ....*.
gi 639298814 584 KLRQAL 589
Cdd:cd19923  110 TLKEKL 115
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-450 1.24e-10

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: 58.62  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTdHGTVKIQVDLVLEKQLEHTIkISVKDSGPGIENDEIAYLTEPYVQSsagKEKG-GTGLGLAIT 425
Cdd:cd16976    1 IQQVLMNLLQNALDAM-GKVENPRIRIAARRLGGRLV-LVVRDNGPGIAEEHLSRVFDPFFTT---KPVGkGTGLGLSIS 75
                         90       100
                 ....*....|....*....|....*
gi 639298814 426 SRLLEKLSSRLEIASQLGTGSVFSF 450
Cdd:cd16976   76 YGIVEEHGGRLSVANEEGAGARFTF 100
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
500-585 1.27e-10

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: 59.29  E-value: 1.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 500 KIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17615   25 DVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPD---VPVLFLTAKDSVEDRIAGLTAGGDDYVTKP 101

                 ....*.
gi 639298814 580 IKHEKL 585
Cdd:cd17615  102 FSLEEV 107
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
235-425 1.29e-10

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 64.18  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 235 LSTISHEIRTPLNGI-LGSAQLVMNQTSD---TRnkayceaIINSAESL----------------NLLVDKVLDYASLdq 294
Cdd:PRK09470 247 LSDISHELRTPLTRLqLATALLRRRQGESkelER-------IETEAQRLdsmindllvlsrnqqkNHLERETFKANSL-- 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 295 SDEALyeEDVEFKtwlnnlclllsplAEQKQLKFELIcNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHgtvKIQVDLV 374
Cdd:PRK09470 318 WSEVL--EDAKFE-------------AEQMGKSLTVS-APPGPWPINGNPNALASALENIVRNALRYSHT---KIEVAFS 378
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 639298814 375 LEKQlehTIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAIT 425
Cdd:PRK09470 379 VDKD---GLTITVDDDGPGVPEEEREQIFRPFyrVDEARDRESGGTGLGLAIV 428
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
477-585 1.65e-10

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: 59.10  E-value: 1.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIA---IEFMADDEhkIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVL 553
Cdd:cd17552    4 ILVIDDEEDIREVVqacLEKLAGWE--VLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQA-NPETQSIPVI 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17552   81 LLTAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
477-581 1.94e-10

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: 58.75  E-value: 1.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITK---ESPDTPVIVVS 79
                         90       100
                 ....*....|....*....|....*
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIK 581
Cdd:cd17555   80 GAGVMSDAVEALRLGAWDYLTKPIE 104
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-451 2.37e-10

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: 58.21  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTdHGTVKIQVDLVLEKqlehtIKISVKDSGPGIENDEIAYLTEPYVQ--SSAGKEKGGTGLGLAI 424
Cdd:cd16939    1 MARALDNLLRNALRYA-HRTVRIALLVSGGR-----LTLIVEDDGPGIPAAARERVFEPFVRldPSRDRATGGFGLGLAI 74
                         90       100
                 ....*....|....*....|....*...
gi 639298814 425 TSRLLEKLSSRLEIA-SQLGtGSVFSFT 451
Cdd:cd16939   75 VHRVALWHGGHVECDdSELG-GACFRLT 101
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
217-427 2.43e-10

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 62.68  E-value: 2.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 217 LNKLADKAQKDLEIRGLFLSTISHEIRTPLNGILGSAQLvMNQTSDTRnkayCEAIINSAESLNLLVDKVLDYASLDQSD 296
Cdd:PRK10755 123 LNQLVSRLTSTLDQERLFTADVAHELRTPLAGIRLHLEL-LEKQHHID----VAPLIARLDQMMHTVEQLLQLARAGQSF 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 297 EALYEEDVEfktWLNNLCL----LLSPLAEQKQLKFELIcNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHGTvKIQVD 372
Cdd:PRK10755 198 SSGHYQTVK---LLEDVILpsqdELSEMLEQRQQTLLLP-ESAADITVQGDATLLRLLLRNLVENAHRYSPEGS-TITIK 272
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 639298814 373 LVLEkqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSagKEKGGTGLGLAITSR 427
Cdd:PRK10755 273 LSQE---DGGAVLAVEDEGPGIDESKCGELSKAFVRMD--SRYGGIGLGLSIVSR 322
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
328-452 2.49e-10

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 58.68  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 328 FELICNIPEQACY-YCDQQKLRQIIINLVGNAIKFTDHGTVkiqVDLVLEKQLEHtIKISVKDSGPGIENDEIAYLTEPY 406
Cdd:cd16947    1 FQVEINIPDRPIYaNANTEALQRILKNLISNAIKYGSDGKF---LGMTLREDEKH-VYIDIWDKGKGISETEKDHVFERL 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 639298814 407 --VQSSAGKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:cd16947   77 ytLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-430 3.94e-10

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: 57.34  E-value: 3.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHgtvKIQVDLVLEKQLehtIKISVKDSGPGIENDEIAYLTEPY--VQSSAGKEKGGTGLGLAI 424
Cdd:cd16949    1 LARALENVLRNALRYSPS---KILLDISQDGDQ---WTITITDDGPGVPEDQLEQIFLPFyrVDSARDRESGGTGLGLAI 74

                 ....*.
gi 639298814 425 TSRLLE 430
Cdd:cd16949   75 AERAIE 80
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
477-579 7.97e-10

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: 56.40  E-value: 7.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhknqRTPVLAFT 556
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS----AVPVIVLS 76
                         90       100
                 ....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17620   77 ARDEESDKIAALDAGADDYLTKP 99
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
477-579 9.23e-10

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: 56.87  E-value: 9.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAIeFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAF 555
Cdd:cd17618    3 ILIVEDePAIREMIAF-NLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKR-DEMTRDIPIIML 80
                         90       100
                 ....*....|....*....|....
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKP 104
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
235-452 1.01e-09

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 61.02  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 235 LSTISHEIRTPLNGILGSAQlvMNQTSDTRnkAYCEAIINSAESLNL-LVDKVLDYAsldqsdealyeedvefktwLNNL 313
Cdd:COG3290  193 LRAQRHDFRNHLHTISGLLQ--LGEYDEAL--EYIDEISEELQELIDsLLSRIGNPV-------------------LAAL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 314 CLLLSPLAEQKQLKFELICN--IPEQACyycDQQKLRQIIINLVGNAI---KFTDHGTVKIQVDLVLEkqlEHTIKISVK 388
Cdd:COG3290  250 LLGKAARARERGIDLTIDIDsdLPDLPL---SDTDLVTILGNLLDNAIeavEKLPEEERRVELSIRDD---GDELVIEVE 323
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814 389 DSGPGIENDEIAYLTEPYVQSsagKEKGGTGLGLAITSRLLEKLSSRLEIASQLGTGSVFSFTV 452
Cdd:COG3290  324 DSGPGIPEELLEKIFERGFST---KLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
477-586 1.12e-09

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 61.40  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhknQRTPVLAFT 556
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHE---TRTPVILMT 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLR 586
Cdd:PRK11361  84 AYAEVETAVEALRCGAFDYVIKPFDLDELN 113
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
477-579 1.79e-09

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 55.77  E-value: 1.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKNQRTPVLAF 555
Cdd:cd17623    1 ILLIDDdRELTELLT-EYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELR----KTSQVPVLML 75
                         90       100
                 ....*....|....*....|....
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17623   76 TARGDDIDRILGLELGADDYLPKP 99
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
477-589 1.94e-09

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 58.67  E-value: 1.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIaIEFMADDEHKIKL---AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrtPVL 553
Cdd:COG3279    4 ILIVDDEPLARER-LERLLEKYPDLEVvgeASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPP----PPI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 639298814 554 AFTASLSpdevkEYLELGIK----DIVGKPIKHEKLRQAL 589
Cdd:COG3279   79 IFTTAYD-----EYALEAFEvnavDYLLKPIDEERLAKAL 113
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
477-557 2.72e-09

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: 55.30  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDlDLNQKIAI-EFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAF 555
Cdd:cd17554    3 ILVVDD-EENIRELYkEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIRE---KKPDLPVIIC 78

                 ..
gi 639298814 556 TA 557
Cdd:cd17554   79 TA 80
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-449 6.66e-09

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: 53.94  E-value: 6.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTD--HGTVKI------QVDLVLEKQlEHTIKISVKDSGPGIENDEIAYLTEPYVqssAGKEkGGT 418
Cdd:cd16918    1 LIQVFLNLVRNAAQALAgsGGEIILrtrtqrQVTLGHPRH-RLALRVSVIDNGPGIPPDLQDTIFYPMV---SGRE-NGT 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 639298814 419 GLGLAITSRLLEKLSSRLEIASQLGTgSVFS 449
Cdd:cd16918   76 GLGLAIAQNIVSQHGGVIECDSQPGH-TVFS 105
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
477-589 6.86e-09

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: 54.10  E-value: 6.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhknQRTPVLAFT 556
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID---ENIRVIIMT 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17553   80 AYGELDMIQESKELGALTHFAKPFDIDEIRDAV 112
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
500-580 7.17e-09

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: 54.20  E-value: 7.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 500 KIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFTAslSPDEVKEY--LELGIKDIVG 577
Cdd:cd19937   23 EVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRS-DPKTSSIPIIMLTA--KGEEFDKVlgLELGADDYIT 99

                 ...
gi 639298814 578 KPI 580
Cdd:cd19937  100 KPF 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
477-585 1.03e-08

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 53.57  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDlDLNQKIAIEFMADDEHKIKLAKD-GKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhkNQRTPVLAF 555
Cdd:cd17616    1 VLLIED-DSATAQSIELMLKSEGFNVYTTDlGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLA---KVKTPILIL 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17616   77 SGLADIEDKVKGLGFGADDYMTKPFHKDEL 106
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
477-529 1.07e-08

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: 51.80  E-value: 1.07e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 639298814   477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLP 529
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
496-585 1.43e-08

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


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 53.27  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 496 DDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAFTASLSPDEVKEYLELGIKD 574
Cdd:cd17550   19 EDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPD---LPVIMISGHGTIETAVKATKLGAYD 95
                         90
                 ....*....|.
gi 639298814 575 IVGKPIKHEKL 585
Cdd:cd17550   96 FIEKPLSLDRL 106
PRK10337 PRK10337
sensor protein QseC; Provisional
217-428 1.56e-08

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 57.74  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 217 LNKLADKAQKDL--EIRglFLSTISHEIRTPLNGIlgSAQLVMNQTSD----TRNKAY--CEAIINSAESLnllVDKVLD 288
Cdd:PRK10337 223 LNQLFARTHAMMvrERR--FTSDAAHELRSPLAAL--KVQTEVAQLSDddpqARKKALlqLHAGIDRATRL---VDQLLT 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 289 YASLDqSDEALyeEDVEFKTWLNnlcLLLSPLAEQ----KQLKFELICNIPEQACYYCDQQKLRQIII-NLVGNAIKFTD 363
Cdd:PRK10337 296 LSRLD-SLDNL--QDVAEIPLED---LLQSAVMDIyhtaQQAGIDVRLTLNAHPVIRTGQPLLLSLLVrNLLDNAIRYSP 369
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639298814 364 HGTvkiQVDLVLEKQLehtikISVKDSGPGIENDEIAYLTEPYVQSSaGKEKGGTGLGLAITSRL 428
Cdd:PRK10337 370 QGS---VVDVTLNARN-----FTVRDNGPGVTPEALARIGERFYRPP-GQEATGSGLGLSIVRRI 425
PRK10693 PRK10693
two-component system response regulator RssB;
503-589 2.51e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.15  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 503 LAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKriDHKNQrTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKH 582
Cdd:PRK10693   2 LAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLR--NRGDQ-TPVLVISATENMADIAKALRLGVQDVLLKPVKD 78

                 ....*...
gi 639298814 583 -EKLRQAL 589
Cdd:PRK10693  79 lNRLREMV 86
pleD PRK09581
response regulator PleD; Reviewed
477-581 2.62e-08

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 56.83  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAiefmaddehKIKL---------AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKN 547
Cdd:PRK09581   5 ILVVDDIPANVKLL---------EAKLlaeyytvltASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLK----SD 71
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 639298814 548 QRT---PVLAFTASLSPDEVKEYLELGIKDIVGKPIK 581
Cdd:PRK09581  72 PATthiPVVMVTALDDPEDRVRGLEAGADDFLTKPIN 108
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
475-604 2.69e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 56.96  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhkNQRTPVLA 554
Cdd:PRK10365   6 IDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKAL---NPAIPVLI 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSDSQSNqTASIAVEL 604
Cdd:PRK10365  83 MTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALAH-THSIDAET 131
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
343-439 3.69e-08

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: 51.69  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFT-DHGTVKIQvdlvLEKQLEHtIKISVKDSGPGIENDEIAYLTEPYVQ-SSAGKEKGGTGL 420
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSpEGGLIALQ----LEADTEG-IELLVFDEGSGIPDYALNRVFERFYSlPRPHSGQKSTGL 75
                         90
                 ....*....|....*....
gi 639298814 421 GLAITSRLLEKLSSRLEIA 439
Cdd:cd16945   76 GLAFVQEVAQLHGGRITLR 94
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
211-447 1.16e-07

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 55.08  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 211 ERREQHL----NKLADKAQkdLEIRGLFLSTISHEIRTPLNGI---LGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLV 283
Cdd:COG4192  411 KRIEKNLrqtqDELIQAAK--MAVVGQTMTSLAHELNQPLNAMsmyLFSAKKALEQENYAQLPTSLDKIEGLIERMDKII 488
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 284 dKVLDYASlDQSDEALYEEDVefKTWLNNLCLLLSPLAEQKQLKFelicNIPEQACYYCDQQKLRQIIINLVGNAIKFTD 363
Cdd:COG4192  489 -KSLRQFS-RKSDTPLQPVDL--RQVIEQAWELVESRAKPQQITL----HIPDDLMVQGDQVLLEQVLVNLLVNALDAVA 560
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 364 HgTVKIQVDLVLEkqlEHTIKISVKDSGPGIENDEiaYLTEPYVQSsagKEKGgTGLGLAITSRLLEKLSSRLEIASQLG 443
Cdd:COG4192  561 T-QPQISVDLLSN---AENLRVAISDNGNGWPLVD--KLFTPFTTT---KEVG-LGLGLSICRSIMQQFGGDLYLASTLE 630

                 ....
gi 639298814 444 TGSV 447
Cdd:COG4192  631 RGAM 634
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
506-586 1.19e-07

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: 50.70  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 506 DGKSAIELM--QAHHFDVVLLDMNLPDLTGQEVLKRLkridHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHE 583
Cdd:cd17584   30 DAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELI----RLEMDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIE 105

                 ...
gi 639298814 584 KLR 586
Cdd:cd17584  106 DLK 108
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
475-589 1.24e-07

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: 50.48  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQA--HHFDVVLLDMNLPDLTGQEVLKRLKRIDHKNQRTPV 552
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaeHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPLI 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 639298814 553 LAFTASLSpDEVKEY-LELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd19933   81 VALTANTD-DSTREKcLSLGMNGVITKPVSLHALGDEL 117
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
477-598 1.25e-07

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 52.23  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDhknQRTPVLAFT 556
Cdd:COG4567    7 LLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERD---PDARIVVLT 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSDSQSNQTA 598
Cdd:COG4567   84 GYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPA 125
PRK11517 PRK11517
DNA-binding response regulator HprR;
475-585 1.73e-07

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 52.59  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKNQRTPVLA 554
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR----TAKQTPVIC 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:PRK11517  77 LTARDSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
504-590 1.95e-07

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: 50.23  E-value: 1.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrtPVLAF-TAslspdeVKEY----LELGIKDIVGK 578
Cdd:cd17532   30 AENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKP----PLIVFvTA------YDEYaveaFELNAVDYLLK 99
                         90
                 ....*....|..
gi 639298814 579 PIKHEKLRQALS 590
Cdd:cd17532  100 PFSEERLAEALA 111
PRK10610 PRK10610
chemotaxis protein CheY;
475-590 2.04e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 50.36  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMAD-DEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLkRIDHKNQRTPVL 553
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKElGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTI-RADGAMSALPVL 84
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALS 590
Cdd:PRK10610  85 MVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLN 121
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
477-579 3.77e-07

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 48.73  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDlNQKIAIEFMADDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKNQRTPVLAF 555
Cdd:cd17621    1 VLVVEDEE-SFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLR----ARSNVPVIMV 75
                         90       100
                 ....*....|....*....|....
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17621   76 TAKDSEIDKVVGLELGADDYVTKP 99
PRK15479 PRK15479
transcriptional regulator TctD;
501-597 4.20e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 51.26  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 501 IKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPI 580
Cdd:PRK15479  27 VDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRK---RGQTLPVLLLTARSAVADRVKGLNVGADDYLPKPF 103
                         90       100
                 ....*....|....*....|....*
gi 639298814 581 KHEKL--------RQALSDSQSNQT 597
Cdd:PRK15479 104 ELEELdarlrallRRSAGQVQEVQQ 128
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
477-540 5.51e-07

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: 49.12  E-value: 5.51e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 639298814 477 VLLVEDLDLnQKIAIEFMADDEHKIKL---AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRL 540
Cdd:COG2197    4 VLIVDDHPL-VREGLRALLEAEPDIEVvgeAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
477-585 6.10e-07

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 48.57  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlNQKIA--IEFMADDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHknqrTPVL 553
Cdd:cd17614    1 ILVVDD---EKPISdiLKFNLTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTSN----VPII 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17614   74 MLTAKDSEVDKVLGLELGADDYVTKPFSNREL 105
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
350-453 6.66e-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: 6.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 350 IIINLVGNAIK-FTDHGTVKIQVDLVLeKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKggtGLGLAITSRL 428
Cdd:cd16915    4 IVGNLIDNALDaLAATGAPNKQVEVFL-RDEGDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER---GIGLALVRQS 79
                         90       100
                 ....*....|....*....|....*
gi 639298814 429 LEKLSSRLEIASQLGTGSVFSFTVT 453
Cdd:cd16915   80 VERLGGSITVESEPGGGTTFSIRIP 104
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
477-579 7.09e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 50.73  E-value: 7.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDldlNQKIA---IEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhkNQRTPVL 553
Cdd:PRK11083   6 ILLVED---EQAIAdtlVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAF---HPALPVI 79
                         90       100
                 ....*....|....*....|....*...
gi 639298814 554 AFTAslSPDEVKEY--LELGIKDIVGKP 579
Cdd:PRK11083  80 FLTA--RSDEVDRLvgLEIGADDYVAKP 105
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
503-585 7.32e-07

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: 48.45  E-value: 7.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 503 LAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLkRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKH 582
Cdd:cd17562   29 EAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKEL-RKLPAYKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDP 107

                 ...
gi 639298814 583 EKL 585
Cdd:cd17562  108 EQL 110
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-430 7.51e-07

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: 48.34  E-value: 7.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVKIQVDLVLEKQlehTIKISVKDSGPGIENDEIAYLTEP-YVQSSAGKEKG-GTGLGLAI 424
Cdd:cd16953    1 LGQVLRNLIGNAISFSPPDTGRITVSAMPTGK---MVTISVEDEGPGIPQEKLESIFDRfYTERPANEAFGqHSGLGLSI 77

                 ....*.
gi 639298814 425 TSRLLE 430
Cdd:cd16953   78 SRQIIE 83
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
501-585 1.02e-06

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: 48.15  E-value: 1.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 501 IKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhkNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPI 580
Cdd:cd17627   25 VETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA---GNDLPILVLTARDSVSDRVAGLDAGADDYLVKPF 101

                 ....*
gi 639298814 581 KHEKL 585
Cdd:cd17627  102 ALEEL 106
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
477-589 1.37e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 49.64  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEF--MADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLA 554
Cdd:PRK10651   9 ILLIDDHPMLRTGVKQLisMAPDITVVGEASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLRE---KSLSGRIVV 85
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:PRK10651  86 FSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKAL 120
ActS_PrrB_HisK NF033792
ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, ...
353-439 1.55e-06

ActS/PrrB/RegB family redox-sensitive histidine kinase; This redox-responsive histidine kinase, found in alpha-proteobacteria, shows strong sequence conservation, including the notable motif [VA]AAAAHELGTPxTI. It always acts as a partner to an ActR/PrrA/RegA family global response regulator transcription factor in a two-component sensory transduction system. Lineage-specific names and gene symbols given to this histidine kinase reflect downstream regulator changes such as entry into stationary phase, anaerobic expression of photosynthesis genes, and survival of exposure to low pH.


Pssm-ID: 468186 [Multi-domain]  Cd Length: 423  Bit Score: 50.98  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 353 NLVGNAIKF-TDHGTVKIQVDlvlekqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEK----GGTGLGLAITSR 427
Cdd:NF033792 318 NLIENAVDFaRSTVTVTASWD-------AESVTITIEDDGPGFPPDVLSRIGEPYVTTRRGEERrpggGGLGLGLFIAKT 390
                         90
                 ....*....|..
gi 639298814 428 LLEKLSSRLEIA 439
Cdd:NF033792 391 LLERSGATVTFA 402
PRK09483 PRK09483
response regulator; Provisional
475-542 2.23e-06

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 49.33  E-value: 2.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 639298814 475 LDVLLVEDLDLnQKIAIEFMADDEHKIKL---AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKR 542
Cdd:PRK09483   2 INVLLVDDHEL-VRAGIRRILEDIKGIKVvgeACCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILR 71
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
477-589 4.14e-06

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: 46.11  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQK--IAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLA 554
Cdd:cd19930    1 VLIAEDQEMVRGalAALLELEDDLEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELRE---ELPDTKVLI 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd19930   78 VTTFGRPGYFRRALAAGVDGYVLKDRPIEELADAI 112
PRK10643 PRK10643
two-component system response regulator PmrA;
477-585 4.19e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 48.49  E-value: 4.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:PRK10643   3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQ---KKYTLPVLILT 79
                         90       100
                 ....*....|....*....|....*....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:PRK10643  80 ARDTLEDRVAGLDVGADDYLVKPFALEEL 108
PRK10816 PRK10816
two-component system response regulator PhoP;
477-589 7.81e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 47.81  E-value: 7.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAFT 556
Cdd:PRK10816   3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRS---NDVSLPILVLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL---RQAL 589
Cdd:PRK10816  80 ARESWQDKVEVLSAGADDYVTKPFHIEEVmarMQAL 115
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
234-429 8.31e-06

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 49.36  E-value: 8.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  234 FLSTISHEIRTPLNGILGSAQLVMNQTSDTRNKAYCEAIINSAESLNLLVDKVLDYASLDQSDEALYEEDVEfktwlnnL 313
Cdd:TIGR03785 488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFD-------L 560
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814  314 CLLLSPLAEQKQL-----KFELicNIPEQAC-YYCDQQKLRQIIINLVGNAIKFTDHGTVkIQVDLvleKQLEHTIKISV 387
Cdd:TIGR03785 561 SEVLSGCMQGYQMtyppqRFEL--NIPETPLvMRGSPELIAQMLDKLVDNAREFSPEDGL-IEVGL---SQNKSHALLTV 634
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 639298814  388 KDSGPGIENDEIAYLTEPYV--QSSAGKEKGGTGLGLAItSRLL 429
Cdd:TIGR03785 635 SNEGPPLPEDMGEQLFDSMVsvRDQGAQDQPHLGLGLYI-VRLI 677
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
504-579 8.58e-06

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: 44.84  E-value: 8.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVlkrlkrIDHKNQR---TPVLAFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd19926   28 ARNVKEARELLASEPYDLCLTDMRLPDGSGLEL------VQHIQQRlpqTPVAVITAYGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
506-585 1.07e-05

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: 45.15  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 506 DGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17626   32 DGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR----AESGVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
496-543 1.86e-05

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: 44.32  E-value: 1.86e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 639298814 496 DDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRI 543
Cdd:cd17569   22 REGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRER 69
REC_1_GGDEF cd19921
first phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
477-578 2.66e-05

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: 44.09  E-value: 2.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADD-EHKIKLAKDGKSAIELMQAHH-FDVVLLDMNLPDLTGQEVLKRLkrIDHKnqrTPVLA 554
Cdd:cd19921    2 VLIVEDSKTFSKVLKHLIAQElGLEVDVAETLAEAKALLEEGDdYFAALVDLNLPDAPNGEAVDLV--LEKG---IPVIV 76
                         90       100
                 ....*....|....*....|....
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGK 578
Cdd:cd19921   77 LTGSFDEDKRETLLSKGVVDYVLK 100
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
477-579 2.88e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 46.80  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLnqkiAIEFM-----ADDEHKIK-LAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhknQR- 549
Cdd:PRK12555   3 IGIVNDSPL----AVEALrralaRDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMA-----ERp 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 639298814 550 TPVLAFTASLS--PDEVKEYLELGIKDIVGKP 579
Cdd:PRK12555  74 CPILIVTSLTErnASRVFEAMGAGALDAVDTP 105
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
477-544 3.66e-05

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: 43.59  E-value: 3.66e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRID 544
Cdd:cd17563    3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQ 70
ompR PRK09468
osmolarity response regulator; Provisional
493-579 3.86e-05

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 45.74  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 493 FMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridHKNQRTPVLAFTAslSPDEVKEY--LEL 570
Cdd:PRK09468  24 YLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLR---SQNNPTPIIMLTA--KGEEVDRIvgLEI 98

                 ....*....
gi 639298814 571 GIKDIVGKP 579
Cdd:PRK09468  99 GADDYLPKP 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
504-579 3.99e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 46.30  E-value: 3.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIdhknQRTPVLAFTaSLSPDEVK---EYLELGIKDIVGKP 579
Cdd:PRK00742  35 APDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRL----RPTPVVMVS-SLTERGAEitlRALELGAVDFVTKP 108
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
477-589 4.11e-05

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: 43.56  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKI-KLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGqevLKRLKRIDHKNQrTPVLAF 555
Cdd:cd19932    3 VLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDG---IEAAKIITSENI-APIVLL 78
                         90       100       110
                 ....*....|....*....|....*....|....
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd19932   79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAI 112
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
354-452 4.20e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 43.18  E-value: 4.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 354 LVGNAIK--FTDHGTV-KIQVDlVLEKQleHTIKISVKDSGPGIENDEIAYLTEPYVQSsagkeKGGTGLGLAITSRLLE 430
Cdd:cd16957    9 LVENAIRhaFPKRKENnEVRVV-VKKDQ--HKVHVSVSDNGQGIPEERLDLLGKTTVTS-----EKGTGTALENLNRRLI 80
                         90       100
                 ....*....|....*....|....*
gi 639298814 431 KL---SSRLEIASQLGTGSVFSFTV 452
Cdd:cd16957   81 GLfgsEACLHIESEVHGGTEVWFVI 105
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
346-423 4.24e-05

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 46.82  E-value: 4.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814  346 KLRQIIINLVGNAIKFTDHGTVKIQVDLVLEKQLEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKG-GTGLGLA 423
Cdd:TIGR02938 387 QLRSLFKALVDNAIEAMNIKGWKRRELSITTALNGDLIVVSILDSGPGIPQDLRYKVFEPFFTTKGGSRKHiGMGLSVA 465
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
477-581 5.34e-05

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: 43.14  E-value: 5.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrtPVLAF 555
Cdd:cd17622    3 ILLVEDdPKLARLIA-DFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG----PILLL 77
                         90       100
                 ....*....|....*....|....*...
gi 639298814 556 TAslSPDEVKEY--LELGIKDIVGKPIK 581
Cdd:cd17622   78 TA--LDSDIDHIlgLELGADDYVVKPVE 103
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
350-460 5.69e-05

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 46.44  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 350 IIIN-LVGNAIK--FTDHGTVKIQVDLVLEkqlEHTIKISVKDSGPGIendeiayltepyvqSSAGKEKGGTGLGLAITS 426
Cdd:COG3920  402 LILNeLVTNALKhaFLSGEGGRIRVSWRRE---DGRLRLTVSDNGVGL--------------PEDVDPPARKGLGLRLIR 464
                         90       100       110
                 ....*....|....*....|....*....|....
gi 639298814 427 RLLEKLSSRLEIASQLGTgsvfSFTVTFTLGELS 460
Cdd:COG3920  465 ALVRQLGGTLELDRPEGT----RVRITFPLAELA 494
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
475-585 6.11e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.92  E-value: 6.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 475 LDVLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridHKNQRTPVLA 554
Cdd:PRK09836   1 MKLLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLR---SANKGMPILL 77
                         90       100       110
                 ....*....|....*....|....*....|.
gi 639298814 555 FTASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:PRK09836  78 LTALGTIEHRVKGLELGADDYLVKPFAFAEL 108
PRK10336 PRK10336
two-component system response regulator QseB;
506-579 6.85e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.89  E-value: 6.85e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639298814 506 DGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:PRK10336  32 QGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWR---EKGQREPVLILTARDALAERVEGLRLGADDYLCKP 102
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
327-456 7.81e-05

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 45.78  E-value: 7.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 327 KFELICNIPEQACYYCDqqkLRQIIINLVGNAIKF-----TDHGTVKIQVdlvleKQLEHTIKISVKDSGPGIENDEIAY 401
Cdd:COG2972  320 RLEVEIEIDEELLDLLI---PKLILQPLVENAIEHgiepkEGGGTIRISI-----RKEGDRLVITVEDNGVGMPEEKLEK 391
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 639298814 402 LtepyvQSSAGKEKGGTGLGLAITSRLLEKL---SSRLEIASQLGTGsvfsFTVTFTL 456
Cdd:COG2972  392 L-----LEELSSKGEGRGIGLRNVRERLKLYygeEYGLEIESEPGEG----TTVTIRI 440
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
477-579 9.91e-05

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 42.37  E-value: 9.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhknQRTPVLAFT 556
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR------EQSEVGIIL 76
                         90       100
                 ....*....|....*....|....*
gi 639298814 557 ASLSPDEVKEY--LELGIKDIVGKP 579
Cdd:cd17619   77 VTGRDDEVDRIvgLEIGADDYVTKP 101
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
477-585 1.43e-04

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: 41.93  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDlDLNQKIAIEFMADDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAF 555
Cdd:cd17598    1 ILIVED-SPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKS-DPDLKDIPVILL 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17598   79 TTLSDPRDVIRGLECGADNFITKPYDEKYL 108
PRK13557 PRK13557
histidine kinase; Provisional
365-589 2.89e-04

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 43.89  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 365 GTVKIQV--------DLVLEKQLE--HTIKISVKDSGPGIENDEIAYLTEPYVQSsagKEKG-GTGLGLAITSRLLEKLS 433
Cdd:PRK13557 297 GRVTIRTrnveiedeDLAMYHGLPpgRYVSIAVTDTGSGMPPEILARVMDPFFTT---KEEGkGTGLGLSMVYGFAKQSG 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 434 SRLEIASQLGTGSVFSFTVTFTLGELSLVEQRHQTKDYLTGLD-VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIE 512
Cdd:PRK13557 374 GAVRIYSEVGEGTTVRLYFPASDQAENPEQEPKARAIDRGGTEtILIVDDRPDVAELARMILEDFGYRTLVASNGREALE 453
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 513 LMQAH-HFDVVLLDMNLP-DLTG----QEVLKRLKRIDhknqrtpVLAFT----ASLSPDEV--KEYlelgikDIVGKPI 580
Cdd:PRK13557 454 ILDSHpEVDLLFTDLIMPgGMNGvmlaREARRRQPKIK-------VLLTTgyaeASIERTDAggSEF------DILNKPY 520
                        250
                 ....*....|...
gi 639298814 581 KHEKL----RQAL 589
Cdd:PRK13557 521 RRAELarrvRMVL 533
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
477-589 2.94e-04

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: 41.18  E-value: 2.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQK-IA--IEfMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVL 553
Cdd:cd19931    1 VLLIDDHPLLRKgIKqlIE-LDPDFTVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALRE---EGVSARIV 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd19931   77 ILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEAL 112
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
347-449 3.32e-04

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: 40.83  E-value: 3.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHG---TVKIQVDLVLEKQLEHT--------IKISVKDSGPGIENDEIAYLTEPYVQSsagKEK 415
Cdd:cd16919    1 LELAILNLAVNARDAMPEGgrlTIETSNQRVDADYALNYrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPFFTT---KEV 77
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 639298814 416 G-GTGLGLAITSRLLEKLSSRLEIASQLGTGSVFS 449
Cdd:cd16919   78 GkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
347-453 3.49e-04

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: 40.45  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 347 LRQIIINLVGNAIKFTDHGTVkIQVDLVLEkqlEHTIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGGTGLGLAITS 426
Cdd:cd16923    1 LQRVFSNLLSNAIKYSPENTR-IYITSFLT---DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGAGLGLSIAK 76
                         90       100
                 ....*....|....*....|....*..
gi 639298814 427 RLLEKLSSRLEIaSQLGTGSVFSFTVT 453
Cdd:cd16923   77 AIIELHGGSASA-EYDDNHDLFKVRLP 102
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
477-579 4.03e-04

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: 40.44  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHknqrTPVLAFT 556
Cdd:cd19938    2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD----VPIIMVT 77
                         90       100
                 ....*....|....*....|....*
gi 639298814 557 ASLspDEVKEY--LELGIKDIVGKP 579
Cdd:cd19938   78 ARV--EEIDRLlgLELGADDYICKP 100
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
354-454 4.06e-04

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


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 40.67  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 354 LVGNAIKFTDHGTVKIQVDLVLEkQLEHTIKISVKDSGPGIENDEIAyltEPYvqssagKEKGGTGLGLAitsrLLEKLS 433
Cdd:COG2172   42 AVTNAVRHAYGGDPDGPVEVELE-LDPDGLEIEVRDEGPGFDPEDLP---DPY------STLAEGGRGLF----LIRRLM 107
                         90       100
                 ....*....|....*....|.
gi 639298814 434 SRLEIASQLGtGSVFSFTVTF 454
Cdd:COG2172  108 DEVEYESDPG-GTTVRLVKRL 127
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
310-443 4.45e-04

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


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 41.08  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 310 LNNLCLLLSPLAEQKQlkFELICNIPEQACYYCDQQKLRQIIINLVGNAIKFTDHgtvkiQVDLVLeKQLEHTIKISVKD 389
Cdd:cd16954    3 LDSLCSALNKVYQRKG--VSISLDISPELRFPGERNDLMELLGNLLDNACKWCLE-----FVEVTA-RQTDGGLHLIVDD 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 639298814 390 SGPGIENDEIAYLTEPYVQssAGKEKGGTGLGLAITSRLLEKLSSRLEIA-SQLG 443
Cdd:cd16954   75 DGPGVPESQRSKIFQRGQR--LDEQRPGQGLGLAIAKEIVEQYGGELSLSdSPLG 127
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
477-557 9.39e-04

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 39.78  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKnqrTPVLAF 555
Cdd:cd17549    1 VLLVDDdADVREALQ-QTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPD---LPVILI 76

                 ..
gi 639298814 556 TA 557
Cdd:cd17549   77 TG 78
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
477-543 1.01e-03

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: 39.25  E-value: 1.01e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAH-HFDVVLLDMNLPD-LTGQEVLKRLKRI 543
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPGgMNGSQLAEEARRR 69
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
477-585 1.08e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 41.24  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLAFT 556
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKR-ESMTRDIPVVMLT 83
                         90       100
                 ....*....|....*....|....*....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:PRK10161  84 ARGEEEDRVRGLETGADDYITKPFSPKEL 112
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
477-579 1.15e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 38.95  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-LDLNQKIAiEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhKNQRTPVLAF 555
Cdd:cd17573    1 ILLIEDdSTLGKEIS-KGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLPDGNGLSIVSRIKE---KHPSIVVIVL 76
                         90       100
                 ....*....|....*....|....
gi 639298814 556 TASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17573   77 SDNPKTEQEIEAFKEGADDYIAKP 100
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
504-579 1.38e-03

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: 38.74  E-value: 1.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298814 504 AKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKNQRTpVLAFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17561   33 AHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPK-IIMLTAFGQEDITQRAVELGASYYILKP 107
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
343-438 1.65e-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: 38.60  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFT-DHGTVKIQVDlvLEKQLehtIKISVKDSGPGIENDEIAYLTEPYVQSSAGKEKGG-TGL 420
Cdd:cd16975    1 DTLLLSRALINIISNACQYApEGGTVSISIY--DEEEY---LYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhYGM 75
                         90
                 ....*....|....*...
gi 639298814 421 GLAITSRLLEKLSSRLEI 438
Cdd:cd16975   76 GLYIAKNLVEKHGGSLII 93
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
501-589 1.78e-03

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: 38.78  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 501 IKLAKDGKSAIELMQAHHFDVVLLDMNLPD-LTGQEVLKRLKridHKNQRTPVLAF---TASLSPDEVKEYLELGIKDIV 576
Cdd:cd17589   26 IDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELR---HKKLISPSTVFimvTGESSRAMVLSALELEPDDYL 102
                         90
                 ....*....|...
gi 639298814 577 GKPIKHEKLRQAL 589
Cdd:cd17589  103 LKPFTVSELRERL 115
HATPase_RsbT-like cd16934
Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...
343-447 1.93e-03

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine/threonine-protein kinase RsbT, and related domains; This family includes the histidine kinase-like ATPase (HATPase) domain of Bacillus subtilis serine/threonine-protein kinase RsbT, a component of the stressosome signaling complex of Bacillus subtilis. The stressosome is formed from multiple copies of three proteins, a sensor protein RsbR, a scaffold protein RsbS, and RsbT, and responds to environmental changes by initiating a protein partner switching cascade. Stress perception increases the phosphorylation of RsbR and RsbS, by RsbT. Subsequent dissociation of RsbT from the stressosome activates the sigma-B cascade, leading to the release of the alternative sigma factor, sigma-B.


Pssm-ID: 340411 [Multi-domain]  Cd Length: 117  Bit Score: 38.51  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 343 DQQKLRQIIINLVGNAIKFTDHGTVKIQVDLVLEKqleHTIKISVKDSGPGiendeIAYLTEpyVQSSAGKEKGGTGLGL 422
Cdd:cd16934   22 RQAEIATAVTELARNLLKHAGGGQVLLEVVAEGGR---VALEILAVDQGPG-----IADVDE--ALRDGFSTGGGLGLGL 91
                         90       100
                 ....*....|....*....|....*
gi 639298814 423 AITSRLLEKLSsrleIASQLGTGSV 447
Cdd:cd16934   92 GGVRRLADEFD----LHSAPGRGTV 112
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
477-579 1.98e-03

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: 38.15  E-value: 1.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQ--AHHFDVVLLDMNLPDLTGQEVLKRLKRidHKN-QRTPVL 553
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdeQNEIDLILTEVDLPVSSGFKLLSYIMR--HKIcKNIPVI 78
                         90       100
                 ....*....|....*....|....*.
gi 639298814 554 AFTASLSPDEVKEYLELGIKDIVGKP 579
Cdd:cd17582   79 MMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
477-589 2.60e-03

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: 38.16  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVED-----LDLnqKIAIEFMAddeHKI-KLAKDGKSAIELMQAHHFDVVLLDMNLP-DLTGQEVLKRLKridhKNQR 549
Cdd:cd17534    3 ILIVEDeaiiaLDL--KEILESLG---YEVvGIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR----EKFD 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 639298814 550 TPVLAFTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQAL 589
Cdd:cd17534   74 IPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
504-585 2.97e-03

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: 38.27  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 504 AKDGKSAIELMQAH-HFDVVLLDMNLPDLTGQEVLKRLkRIDHKNQRTPVLAFTASLSPDEVKEYLELGIKDIVGKPIKH 582
Cdd:cd17544   30 AANGQEALEVLEQHpDIKLVITDYNMPEMDGFELVREI-RKKYSRDQLAIIGISASGDNALSARFIKAGANDFLTKPFLP 108

                 ...
gi 639298814 583 EKL 585
Cdd:cd17544  109 EEF 111
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
477-585 3.46e-03

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 37.81  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRidhkNQRTPVLAFT 556
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRA----RSDVPIIIIS 77
                         90       100       110
                 ....*....|....*....|....*....|
gi 639298814 557 ASLSPDEVKEY-LELGIKDIVGKPIKHEKL 585
Cdd:cd17594   78 GDRRDEIDRVVgLELGADDYLAKPFGLREL 107
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
477-585 3.56e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.06  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKiAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHKNQrTPVLAFT 556
Cdd:cd17539    1 VLLVDDRPSSAE-RIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQ-LPILAVA 78
                         90       100
                 ....*....|....*....|....*....
gi 639298814 557 ASLSPDEVKEYLELGIKDIVGKPIKHEKL 585
Cdd:cd17539   79 DPGDRGRLIRALEIGVNDYLVRPIDPNEL 107
fixJ PRK09390
response regulator FixJ; Provisional
473-598 3.59e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 39.22  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 473 TGLDVLLVEDLDLNQKIAIEFMAD-DEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRIDHknqRTP 551
Cdd:PRK09390   1 SDKGVVHVVDDDEAMRDSLAFLLDsAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKARGS---PLP 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 639298814 552 VLAFTASLS-PDEVkEYLELGIKDIVGKPIKHEKL----RQALsdSQSNQTA 598
Cdd:PRK09390  78 VIVMTGHGDvPLAV-EAMKLGAVDFIEKPFEDERLigaiERAL--AQAPEAA 126
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
477-579 3.98e-03

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: 37.42  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDlDLNQKIAIEFMADDE-HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKridhKNQRTPVLAF 555
Cdd:cd19936    1 IALVDD-DRNILTSVSMALEAEgFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR----QKSTLPVIFL 75
                         90       100
                 ....*....|....*....|....*.
gi 639298814 556 TAslSPDEVKEY--LELGIKDIVGKP 579
Cdd:cd19936   76 TS--KDDEIDEVfgLRMGADDYITKP 99
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
477-544 6.32e-03

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: 36.71  E-value: 6.32e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDEHKIKLAKDGKSAIELM-QAHHFDVVLLDMNLPDLTGQEVLKRLKRID 544
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKID 70
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
350-449 7.56e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 39.51  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 350 IIINLVGNAIKFTDhGTVKIQVDLVLEKQLEHtIKISVKDSGPGIENDEIAYLtepYVQ--SSAGKEKGgtgLGLAITSR 427
Cdd:PRK11086 437 ILGNLIENALEAVG-GEEGGEISVSLHYRNGW-LHCEVSDDGPGIAPDEIDAI---FDKgySTKGSNRG---VGLYLVKQ 508
                         90       100
                 ....*....|....*....|..
gi 639298814 428 LLEKLSSRLEIASQLGTGSVFS 449
Cdd:PRK11086 509 SVENLGGSIAVESEPGVGTQFF 530
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
477-591 8.89e-03

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 38.29  E-value: 8.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639298814 477 VLLVEDLDLNQKIAIEFMADDE--HKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKRiDHKNQRTPVLa 554
Cdd:PRK10403   9 VLIVDDHPLMRRGVRQLLELDPgfEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRR-DGVTAQIIIL- 86
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 639298814 555 fTASLSPDEVKEYLELGIKDIVGKPIKHEKLRQALSD 591
Cdd:PRK10403  87 -TVSDASSDVFALIDAGADGYLLKDSDPEVLLEAIRA 122
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
477-542 9.77e-03

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


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 36.96  E-value: 9.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 639298814 477 VLLVEDlDLNQKIAIEFMADDEHKIKLAKDGKSAIELMQAHHFDVVLLDMNLPDLTGQEVLKRLKR 542
Cdd:cd17596    3 ILVVDD-EVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRE 67
 
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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