NCBI Conserved Domain Search

Conserved domains on [gi|15598240|ref|NP_251734|]

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two-component sensor [Pseudomonas aeruginosa PAO1]

Protein Classification

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 ...

235-728

1.17e-88

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: 299.00 E-value: 1.17e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   235 REAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQR-LAPEQREraSLEVAYEAAGSLQLLIGDILDVAKIESG 313
Cdd:TIGR02956 451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTgLTSQQQQ--YLQVINRSGESLLDILNDILDYSKIEAG 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   314 HLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIRLqerS 393
Cdd:TIGR02956 529 HLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV---S 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   394 LDEGRAIvRVDVEDSGIGIAPADQARLFQPFIQvAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLL 473
Cdd:TIGR02956 606 LNDDSSL-LFEVEDTGCGIAEEEQATLFDAFTQ-ADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   474 RQCGPKmpESGQDPLAASMEPsrrLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPR 553
Cdd:TIGR02956 684 TRGKPA--EDSATLTVIDLPP---QRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPD 758

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   554 LNGYQLARRIRIQERCERRAPilILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA------------------ 615
Cdd:TIGR02956 759 GDGVTLLQQLRAIYGAKNEVK--FIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAvilaggksnteapvlsas 836

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   616 ----TSFGRDAAQPRGLYDAAALSS-------LGGD----RPERLRELLETLLGSNRQDLQRLAILLREGDRTRLAEHAH 680
Cdd:TIGR02956 837 psfdSASVIENAQADDIPESNQASEflldeeqLQQDievlGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAH 916

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598240   681 RIKGAARMIGARTLLEACEALE----DACRRSGDGECLQAPGERLRLALEAL 728
Cdd:TIGR02956 917 KLKGSAGSLGLTQLTQLCQQLEkqgkTGALELSDIDEIKQAWQASKTALDQW 968

PAS super family

cl43642

PAS domain [Signal transduction mechanisms];

102-261

2.53e-10

PAS domain [Signal transduction mechanisms];

The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 61.58 E-value: 2.53e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQcLAVARG 181
Cdd:COG2202   1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLR-AALAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 182 GTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRT 261
Cdd:COG2202  80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159

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 ...

235-728

1.17e-88

Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 299.00 E-value: 1.17e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   235 REAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQR-LAPEQREraSLEVAYEAAGSLQLLIGDILDVAKIESG 313
Cdd:TIGR02956 451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTgLTSQQQQ--YLQVINRSGESLLDILNDILDYSKIEAG 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   314 HLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIRLqerS 393
Cdd:TIGR02956 529 HLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV---S 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   394 LDEGRAIvRVDVEDSGIGIAPADQARLFQPFIQvAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLL 473
Cdd:TIGR02956 606 LNDDSSL-LFEVEDTGCGIAEEEQATLFDAFTQ-ADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   474 RQCGPKmpESGQDPLAASMEPsrrLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPR 553
Cdd:TIGR02956 684 TRGKPA--EDSATLTVIDLPP---QRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPD 758

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   554 LNGYQLARRIRIQERCERRAPilILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA------------------ 615
Cdd:TIGR02956 759 GDGVTLLQQLRAIYGAKNEVK--FIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAvilaggksnteapvlsas 836

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   616 ----TSFGRDAAQPRGLYDAAALSS-------LGGD----RPERLRELLETLLGSNRQDLQRLAILLREGDRTRLAEHAH 680
Cdd:TIGR02956 837 psfdSASVIENAQADDIPESNQASEflldeeqLQQDievlGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAH 916

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598240   681 RIKGAARMIGARTLLEACEALE----DACRRSGDGECLQAPGERLRLALEAL 728
Cdd:TIGR02956 917 KLKGSAGSLGLTQLTQLCQQLEkqgkTGALELSDIDEIKQAWQASKTALDQW 968

PRK09959

acid-sensing system histidine kinase EvgS;

78-702

2.11e-88

acid-sensing system histidine kinase EvgS;

Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 302.04 E-value: 2.11e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240    78 VACLVCVGCLGWNTVLQLRLRRWQRTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNR--------NYLESLRMTR 149
Cdd:PRK09959  542 LSVLLVGSSLLWGFYLLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSafehyftaDYYKNAMLPL 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   150 EQARGTLL-----TDSDWVEGSKARLMHQQCLAVARGgtasftdMAVRIggqlleIHHWVTPYRDRQGRVLGLMNGWIDI 224
Cdd:PRK09959  622 ENSDSPFKdvfsnAHEVTAETKENRTIYTQVFEIDNG-------IEKRC------INHWHTLCNLPASDHAVYICGWQDI 688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   225 TERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVL-QRLAPEQRERAsLEVAYEAAGSLQLLIGD 303
Cdd:PRK09959  689 TETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSgSGLSKEQRVEA-ISLAYATGQSLLGLIGE 767

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   304 ILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERG 383
Cdd:PRK09959  768 ILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEG 847

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   384 QVTIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTvQGGTGLGLAICRKLVDLMGGDVEMHSEPGK 463
Cdd:PRK09959  848 AVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQ-QTGSGLGLMICKELIKNMQGDLSLESHPGI 926

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   464 GTRVSLDL---LLRQCGpKMPESGQDPLAAsmepSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADE 540
Cdd:PRK09959  927 GTTFTITIpveISQQVA-TVEAKAEQPITL----PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQ 1001

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   541 RFEVLISDCNMPRLNGYQLARRIRiqercERRAPILILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLAT--SF 618
Cdd:PRK09959 1002 HYDLLITDVNMPNMDGFELTRKLR-----EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQlhQV 1076

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   619 GRDAAQPRGLyDAAALSSLGGDRPERLRELLETLLGSNRQDLQRLAILLREGDRTRLAEHAHRIKGAARMIGARTLLEAC 698
Cdd:PRK09959 1077 AHIAPQYRHL-DIEALKNNTANDLQLMQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINIS 1155


                  ....
gi 15598240   699 EALE 702
Cdd:PRK09959 1156 HQLE 1159

BaeS

COG0642

Signal transduction histidine kinase [Signal transduction mechanisms];

176-471

8.91e-77

Signal transduction histidine kinase [Signal transduction mechanisms];

Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 250.21 E-value: 8.91e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 176 LAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATM 255
Cdd:COG0642  38 LALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANV 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 256 SHEIRTPMNAVIGILELVLQRLAPEQRERasLEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMF 335
Cdd:COG0642 118 SHELRTPLTAIRGYLELLLEELDEEQREY--LETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELF 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 336 EGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIKFTERG-QVTIRLQErslDEGRaiVRVDVEDSGIGIAP 414
Cdd:COG0642 196 RPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRR---EGDR--VRISVEDTGPGIPP 269

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240 415 ADQARLFQPFIQvAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG0642 270 EDLERIFEPFFR-TDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325

HATPase_EvgS-ArcB-TorS-like

cd16922

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...

365-473

9.06e-53

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: 177.68 E-value: 9.06e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 365 FKQVLSNLVSNAIKFTERGQVTIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGLGLAI 443
Cdd:cd16922   1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTrKYGGTGLGLAI 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15598240 444 CRKLVDLMGGDVEMHSEPGKGTRVSLDLLL 473
Cdd:cd16922  81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110

HATPase_c

smart00387

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

360-474

5.15e-37

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

Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 134.31 E-value: 5.15e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240    360 IDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSLDegraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTG 438
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTG 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 15598240    439 LGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLR 474
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111

HATPase_c

pfam02518

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...

361-475

8.36e-32

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: 119.40 E-value: 8.36e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   361 DPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERsldegrAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRtvQGGTGL 439
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLSEG------GELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG--GGGTGL 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15598240   440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLRQ 475
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109

BaeS_SmeS

NF012163

sensor histidine kinase efflux regulator BaeS;

226-471

2.00e-25

sensor histidine kinase efflux regulator BaeS;

Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 110.30 E-value: 2.00e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELV---LQRLAPEQRERASLEVayeaaGSLQLLIG 302
Cdd:NF012163 218 ELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIqdgIRKFTPESLDSLQAEV-----GTLTKLVD 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  303 DILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPgrDVLIDPLRFKQVLSNLVSNAIKFTER 382
Cdd:NF012163 293 DLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDS 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  383 GQvTIRLQERSLDEGraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGLGLAICRKLVDLMGGDVEMHSEP 461
Cdd:NF012163 371 GG-SLHISASQRPKE---VTLTVADSAPGVSDEQLARLFERFYRVEVSRNrASGGSGLGLAISLNIVQAHGGTLHAAHSP 446

                        250
                 ....*....|
gi 15598240  462 GKGTRVSLDL 471
Cdd:NF012163 447 LGGLRIVVTL 456

MtrAB_MtrB

NF040691

MtrAB system histidine kinase MtrB;

230-471

1.09e-24

MtrAB system histidine kinase MtrB;

Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 108.57 E-value: 1.09e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  230 LARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVigilelvlqRLAPE----QRE------RASLEVAYEAAGSLQL 299
Cdd:NF040691 253 MADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTI---------RMAADvihdSRDdfdpatARSAELLHTELDRFES 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  300 LIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGrDVLIDPLRFKQVLSNLVSNAIKF 379
Cdd:NF040691 324 LLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPV-VAEVDPRRVERVLRNLVVNAIEH 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  380 TERGQVTIRlqersLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQV--AKGRTVqGGTGLGLAICRKLVDLMGGDVEM 457
Cdd:NF040691 403 GEGKPVVVT-----VAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdpARARTT-GGTGLGLAIALEDARLHGGWLEA 476

                        250
                 ....*....|....
gi 15598240  458 HSEPGKGTRVSLDL 471
Cdd:NF040691 477 WGRPGQGSQFRLTL 490

PAS

COG2202

PAS domain [Signal transduction mechanisms];

102-261

2.53e-10

PAS domain [Signal transduction mechanisms];

Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 61.58 E-value: 2.53e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQcLAVARG 181
Cdd:COG2202   1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLR-AALAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 182 GTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRT 261
Cdd:COG2202  80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159

PAS_4

pfam08448

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...

118-229

3.51e-07

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

Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 49.33 E-value: 3.51e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   118 VDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSdWVEGSKARLMHQQCLAVARGGTASFTDMAVRIGgql 197
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLERALRRALEGEEPIDFLEELLLNG--- 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15598240   198 lEIHHW---VTPYRDRQGRVLGLMNGWIDITERER 229
Cdd:pfam08448  77 -EERHYelrLTPLRDPDGEVIGVLVISRDITERRR 110

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 ...

235-728

1.17e-88

Pssm-ID: 274362 [Multi-domain] Cd Length: 968 Bit Score: 299.00 E-value: 1.17e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   235 REAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQR-LAPEQREraSLEVAYEAAGSLQLLIGDILDVAKIESG 313
Cdd:TIGR02956 451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTgLTSQQQQ--YLQVINRSGESLLDILNDILDYSKIEAG 528

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   314 HLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIRLqerS 393
Cdd:TIGR02956 529 HLSISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV---S 605

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   394 LDEGRAIvRVDVEDSGIGIAPADQARLFQPFIQvAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLL 473
Cdd:TIGR02956 606 LNDDSSL-LFEVEDTGCGIAEEEQATLFDAFTQ-ADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPL 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   474 RQCGPKmpESGQDPLAASMEPsrrLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPR 553
Cdd:TIGR02956 684 TRGKPA--EDSATLTVIDLPP---QRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPD 758

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   554 LNGYQLARRIRIQERCERRAPilILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA------------------ 615
Cdd:TIGR02956 759 GDGVTLLQQLRAIYGAKNEVK--FIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAvilaggksnteapvlsas 836

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   616 ----TSFGRDAAQPRGLYDAAALSS-------LGGD----RPERLRELLETLLGSNRQDLQRLAILLREGDRTRLAEHAH 680
Cdd:TIGR02956 837 psfdSASVIENAQADDIPESNQASEflldeeqLQQDievlGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAH 916

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15598240   681 RIKGAARMIGARTLLEACEALE----DACRRSGDGECLQAPGERLRLALEAL 728
Cdd:TIGR02956 917 KLKGSAGSLGLTQLTQLCQQLEkqgkTGALELSDIDEIKQAWQASKTALDQW 968

PRK09959

acid-sensing system histidine kinase EvgS;

78-702

2.11e-88

acid-sensing system histidine kinase EvgS;

Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 302.04 E-value: 2.11e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240    78 VACLVCVGCLGWNTVLQLRLRRWQRTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNR--------NYLESLRMTR 149
Cdd:PRK09959  542 LSVLLVGSSLLWGFYLLRSVRRRKVIQGDLENQISFRKALSDSLPNPTYVVNWQGNVISHNSafehyftaDYYKNAMLPL 621

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   150 EQARGTLL-----TDSDWVEGSKARLMHQQCLAVARGgtasftdMAVRIggqlleIHHWVTPYRDRQGRVLGLMNGWIDI 224
Cdd:PRK09959  622 ENSDSPFKdvfsnAHEVTAETKENRTIYTQVFEIDNG-------IEKRC------INHWHTLCNLPASDHAVYICGWQDI 688

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   225 TERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVL-QRLAPEQRERAsLEVAYEAAGSLQLLIGD 303
Cdd:PRK09959  689 TETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSgSGLSKEQRVEA-ISLAYATGQSLLGLIGE 767

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   304 ILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERG 383
Cdd:PRK09959  768 ILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSCSSTFPDHYLVKIDPQAFKQVLSNLLSNALKFTTEG 847

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   384 QVTIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTvQGGTGLGLAICRKLVDLMGGDVEMHSEPGK 463
Cdd:PRK09959  848 AVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQ-QTGSGLGLMICKELIKNMQGDLSLESHPGI 926

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   464 GTRVSLDL---LLRQCGpKMPESGQDPLAAsmepSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADE 540
Cdd:PRK09959  927 GTTFTITIpveISQQVA-TVEAKAEQPITL----PEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQ 1001

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   541 RFEVLISDCNMPRLNGYQLARRIRiqercERRAPILILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLAT--SF 618
Cdd:PRK09959 1002 HYDLLITDVNMPNMDGFELTRKLR-----EQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQlhQV 1076

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   619 GRDAAQPRGLyDAAALSSLGGDRPERLRELLETLLGSNRQDLQRLAILLREGDRTRLAEHAHRIKGAARMIGARTLLEAC 698
Cdd:PRK09959 1077 AHIAPQYRHL-DIEALKNNTANDLQLMQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINIS 1155


                  ....
gi 15598240   699 EALE 702
Cdd:PRK09959 1156 HQLE 1159

PRK15347

two component system sensor kinase;

224-704

4.82e-79

two component system sensor kinase;

Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 271.90 E-value: 4.82e-79

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  224 ITERerlARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELvLQR--LAPEQRERAslEVAYEAAGSLQLLI 301
Cdd:PRK15347 377 VAER---TQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALEL-LQNtpLTAEQMDLA--DTARQCTLSLLAII 450

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  302 GDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTE 381
Cdd:PRK15347 451 NNLLDFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTE 530

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  382 RGQvtIRLQERSLDEGRAIvrvDVEDSGIGIAPADQARLFQPFIQVAkgrTVQGGTGLGLAICRKLVDLMGGDVEMHSEP 461
Cdd:PRK15347 531 TGG--IRLRVKRHEQQLCF---TVEDTGCGIDIQQQQQIFTPFYQAD---THSQGTGLGLTIASSLAKMMGGELTLFSTP 602

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  462 GKGTRVSLDLLLRQCGPKMPESGQ--DPLA-------------ASME------------PSR------------------ 496
Cdd:PRK15347 603 GVGSCFSLVLPLNEYAPPEPLKGElsAPLAlhrqlsawgitcqPGHQnpalldpelaylPGRlydllqqiiqgapnepvi 682

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  497 -------RLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQER- 568
Cdd:PRK15347 683 nlplqpwQLQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNn 762

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  569 CERRAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATsfgrdAAQPRGLYDAAALSSLGGDRPERLREL 648
Cdd:PRK15347 763 LDPDCMIVAL--TANAAPEEIHRCKKAGMNHYLTKPVTLAQLARALEL-----AAEYQLLRGIELSPQDSSCSPLLDTDD 835

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15598240  649 LETllgsNRQDLQRLAILLRE-----GDRTRLAEHAHRIKGAARMIGARTLLEACEALEDA 704
Cdd:PRK15347 836 MAL----NSKLYQSLLLLLAQieqavENQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENA 892

BaeS

COG0642

Signal transduction histidine kinase [Signal transduction mechanisms];

176-471

8.91e-77

Signal transduction histidine kinase [Signal transduction mechanisms];

Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 250.21 E-value: 8.91e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 176 LAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATM 255
Cdd:COG0642  38 LALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANV 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 256 SHEIRTPMNAVIGILELVLQRLAPEQRERasLEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMF 335
Cdd:COG0642 118 SHELRTPLTAIRGYLELLLEELDEEQREY--LETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELF 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 336 EGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIKFTERG-QVTIRLQErslDEGRaiVRVDVEDSGIGIAP 414
Cdd:COG0642 196 RPLAEEKGIELELDLPDDLPT-VRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVSVRR---EGDR--VRISVEDTGPGIPP 269

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240 415 ADQARLFQPFIQvAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG0642 270 EDLERIFEPFFR-TDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTL 325

PRK11091

aerobic respiration control sensor protein ArcB; Provisional

102-694

2.92e-76

aerobic respiration control sensor protein ArcB; Provisional

Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 261.80 E-value: 2.92e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQ--------------ARGTLLTDSDwVEGSK 167
Cdd:PRK11091 145 ETQIELEQQSSLLRSFLDASPDLVYYRNEDGEFSGCNRAMELLTGKSEKQligltpkdvyspeaAEKVIETDEK-VFRHN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  168 ARLMHQQCLAVARGGTASFtdmavriggqllEIHHwvTPYRDRQGRVLGLMNGWIDITERERLARQLreamrqaDEANRA 247
Cdd:PRK11091 224 VSLTYEQWLDYPDGRKACF------------ELRK--VPFYDRVGKRHGLMGFGRDITERKRYQDAL-------EKASRD 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  248 KSVFLATMSHEIRTPMNAVIGILELVLQ-RLAPEQRerASLEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRH 326
Cdd:PRK11091 283 KTTFISTISHELRTPLNGIVGLSRILLDtELTAEQR--KYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPIDFTD 360

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  327 VVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIRLQErsldEGRAIVRVDVE 406
Cdd:PRK11091 361 FLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRY----EEGDMLTFEVE 436

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  407 DSGIGIAPADQARLFQPFIQV--AKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLrqcgPKMPESG 484
Cdd:PRK11091 437 DSGIGIPEDELDKIFAMYYQVkdSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHA----PAVAEEV 512

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  485 QDPLAASMEPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR 564
Cdd:PRK11091 513 EDAFDEDDMPLPALNILLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELR 592

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  565 IQERCERRAPILILgyTADAEPDEvQRCRDAGMDDCLFKPLGLETLRNYLATSFGRDAAQP------------RGLYDAA 632
Cdd:PRK11091 593 ERYPREDLPPLVAL--TANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDEEstvtteesskanEALLDIP 669

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598240  633 ALSS---LGGDRPErlrelletllgsnRQDLQ--------RLAIL---LREGDRTRLAEHAHRIKGAARMIGARTL 694
Cdd:PRK11091 670 MLEQyveLVGPKLI-------------TDSLAvfekmmpgYLSVLdsnLTARDQKGIVEEAHKIKGAAGSVGLRHL 732

PRK10841

two-component system sensor histidine kinase RcsC;

222-616

8.61e-76

two-component system sensor histidine kinase RcsC;

Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 262.99 E-value: 8.61e-76

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  222 IDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERasLEVAYEAAGSLQL-L 300
Cdd:PRK10841 421 VDVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDR--LVTAMNNSSSLLLkI 498

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  301 IGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELD-DAPgRDVLIDPLRFKQVLSNLVSNAIKF 379
Cdd:PRK10841 499 ISDILDFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEpDVP-VALNGDPMRLQQVISNLLSNAIKF 577

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  380 TERGQVTIRLQersLDEGRAIVRvdVEDSGIGIAPADQARLFQPFIQVAKG--RTVQgGTGLGLAICRKLVDLMGGDVEM 457
Cdd:PRK10841 578 TDTGCIVLHVR---VDGDYLSFR--VRDTGVGIPAKEVVRLFDPFFQVGTGvqRNFQ-GTGLGLAICEKLINMMDGDISV 651

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  458 HSEPGKGTRVS------------------------------------LDLLLRQCG------PKMPESGQD--------- 486
Cdd:PRK10841 652 DSEPGMGSQFTiriplygaqypqkkgveglqgkrcwlavrnasleqfLETLLQRSGiqvqryEGQEPTPEDvlitddpvq 731

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  487 ---PLAASMEPSRR--------------------------------------------------------LHILIADDYP 507
Cdd:PRK10841 732 kkwQGRAVITFCRRhigipleiapgewvhstatphelpallariyrielesddsanalpstdkavsdnddMMILVVDDHP 811

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  508 PNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPilILGYTADAEPD 587
Cdd:PRK10841 812 INRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLRQL---GLTLP--VIGVTANALAE 886

                        490       500
                 ....*....|....*....|....*....
gi 15598240  588 EVQRCRDAGMDDCLFKPLGLETLRNYLAT 616
Cdd:PRK10841 887 EKQRCLEAGMDSCLSKPVTLDVLKQTLTV 915

KdpD

COG2205

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

233-471

8.73e-71

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

Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 231.33 E-value: 8.73e-71

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 233 QLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQR--LAPEQRERaSLEVAYEAAGSLQLLIGDILDVAKI 310
Cdd:COG2205   1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEedLSPEERRE-LLEIIRESAERLLRLIEDLLDLSRL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 311 ESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRL 389
Cdd:COG2205  80 ESGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSpPGGTITISA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 390 QErslDEGRaiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTvQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:COG2205 159 RR---EGDG--VRISVSDNGPGIPEEELERIFERFYRGDNSRG-EGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTV 232


                ..
gi 15598240 470 DL 471
Cdd:COG2205 233 TL 234

WalK

COG5002

Sensor histidine kinase WalK [Signal transduction mechanisms];

176-471

1.83e-69

Sensor histidine kinase WalK [Signal transduction mechanisms];

Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 232.91 E-value: 1.83e-69

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 176 LAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATM 255
Cdd:COG5002  93 LLLLLLLALLILLLLLALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANV 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 256 SHEIRTPMNAVIGILELVLQRLA--PEQRERAsLEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRR 333
Cdd:COG5002 173 SHELRTPLTSIRGYLELLLDGAAddPEERREY-LEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVE 251

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 334 MFEGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQErslDEGRaiVRVDVEDSGIGI 412
Cdd:COG5002 252 ELRPLAEEKGIELELDLPEDPLL-VLGDPDRLEQVLTNLLDNAIKYTpEGGTITVSLRE---EDDQ--VRISVRDTGIGI 325

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 413 APADQARLFQPFIQVAKGRTVQ-GGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG5002 326 PEEDLPRIFERFYRVDKSRSREtGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITL 385

PRK11107

hybrid sensory histidine kinase BarA; Provisional

237-465

5.38e-58

hybrid sensory histidine kinase BarA; Provisional

Pssm-ID: 236848 [Multi-domain] Cd Length: 919 Bit Score: 212.40 E-value: 5.38e-58

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  237 AMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQ-RLAPEQR------ERAslevayeaAGSLQLLIGDILDVAK 309
Cdd:PRK11107 282 AKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKtPLTPTQRdylqtiERS--------ANNLLAIINDILDFSK 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  310 IESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELD-DAPgRDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIR 388
Cdd:PRK11107 354 LEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDpDVP-DNVIGDPLRLQQIITNLVGNAIKFTESGNIDIL 432

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598240  389 LQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAICRKLVDLMGGDVEMHSEPGKGT 465
Cdd:PRK11107 433 VELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRhGGTGLGLVITQKLVNEMGGDISFHSQPNRGS 510

PRK11466

hybrid sensory histidine kinase TorS; Provisional

226-704

8.32e-54

hybrid sensory histidine kinase TorS; Provisional

Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 200.13 E-value: 8.32e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVL-QRLAPEQREraSLEVAYEAAGSLQLLIGDI 304
Cdd:PRK11466 422 ELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLAdNPALNAQRD--DLRAITDSGESLLTILNDI 499

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  305 LDVAKIESG--HLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTER 382
Cdd:PRK11466 500 LDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDE 579

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  383 GqvTIRLQERSLDEGRAIvrvDVEDSGIGIAPADQARLFQPFIQVAKGRtvqGGTGLGLAICRKLVDLMGGDVEMHSEPG 462
Cdd:PRK11466 580 G--SIVLRSRTDGEQWLV---EVEDSGCGIDPAKLAEIFQPFVQVSGKR---GGTGLGLTISSRLAQAMGGELSATSTPE 651

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  463 KGTRVSLDLLLRQCGPKMPESGQDPLAASmepSRRLhiLIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWA-DER 541
Cdd:PRK11466 652 VGSCFCLRLPLRVATAPVPKTVNQAVRLD---GLRL--LLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQnSEP 726

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  542 FEVLISDCNMPRLNGYQLARRIriqerCERRAPILILGYTADAePDEVQRCRDAGM-DDCLFKPLGLETLRNYLATSFGR 620
Cdd:PRK11466 727 FAAALVDFDLPDYDGITLARQL-----AQQYPSLVLIGFSAHV-IDETLRQRTSSLfRGIIPKPVPREVLGQLLAHYLQL 800

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  621 DAAQPRGLYDaaalSSLGGDRPERLRELLETLLGSNRQD----LQRLAILLREGDRTRLAEHAHRIKGAARMIGARTLLE 696
Cdd:PRK11466 801 QVNNDQPLDV----SQLNEDAALMGTEKIHEWLALFKQHalplLDEIDIARASQDSEKIKRAAHQLKSSCSSLGMRQASQ 876


                 ....*...
gi 15598240  697 ACEALEDA 704
Cdd:PRK11466 877 ACAQLEQQ 884

HATPase_EvgS-ArcB-TorS-like

cd16922

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...

365-473

9.06e-53

Pssm-ID: 340399 [Multi-domain] Cd Length: 110 Bit Score: 177.68 E-value: 9.06e-53

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 365 FKQVLSNLVSNAIKFTERGQVTIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGLGLAI 443
Cdd:cd16922   1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTrKYGGTGLGLAI 80

                        90       100       110
                ....*....|....*....|....*....|
gi 15598240 444 CRKLVDLMGGDVEMHSEPGKGTRVSLDLLL 473
Cdd:cd16922  81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110

NtrB

COG3852

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

106-469

1.70e-52

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

Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 185.82 E-value: 1.70e-52

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 106 DLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQqclAVARGGTAS 185
Cdd:COG3852   1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLER---ALAEGQPVT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 186 FTDMAV-RIGGQLLEIHHWVTPYRDRQGRVLGLMNgWIDITERERLARQLREAMRQadEANRAksvFLATMSHEIRTPMN 264
Cdd:COG3852  78 EREVTLrRKDGEERPVDVSVSPLRDAEGEGGVLLV-LRDITERKRLERELRRAEKL--AAVGE---LAAGLAHEIRNPLT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 265 AVIGILELvLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAKIESGHLtltpERVRLRHVVESVRRMFEGLARqKGL 344
Cdd:COG3852 152 GIRGAAQL-LERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPER----EPVNLHEVLERVLELLRAEAP-KNI 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 345 RLVVELDDAPGrDVLIDPLRFKQVLSNLVSNAIK-FTERGQVTIRLQERSLDEGRAI-----VRVDVEDSGIGIAPADQA 418
Cdd:COG3852 226 RIVRDYDPSLP-EVLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQVTLGGLrprlyVRIEVIDNGPGIPEEILD 304

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15598240 419 RLFQPFIqvakgRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:COG3852 305 RIFEPFF-----TTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRI 350

COG4251

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...

87-471

1.84e-47

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

Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 175.74 E-value: 1.84e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  87 LGWNTVLQLRLRRWQRTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGS 166
Cdd:COG4251 112 LLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLL 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 167 KARLMHQQCLAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDIT---------ERERLARQLREA 237
Cdd:COG4251 192 LLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILvlellelrlELEELEEELEER 271

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 238 MRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERA--SLEVAYEAAGSLQLLIGDILDVAKIesGHL 315
Cdd:COG4251 272 TAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEEDYGDKLDEEGreYLERIRDAAERMQALIDDLLAYSRV--GRQ 349

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 316 TLTPERVRLRHVVESVRRMFEGLARQKGLRLVVElddaPGRDVLIDPLRFKQVLSNLVSNAIKFT---ERGQVTIRLQEr 392
Cdd:COG4251 350 ELEFEPVDLNELLEEVLEDLEPRIEERGAEIEVG----PLPTVRGDPTLLRQVFQNLISNAIKYSrpgEPPRIEIGAER- 424

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598240 393 slDEGRaiVRVDVEDSGIGIAPADQARLFQPFiQVAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG4251 425 --EGGE--WVFSVRDNGIGIDPEYAEKIFEIF-QRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTL 498

COG4191

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...

139-471

1.48e-43

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

Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 161.12 E-value: 1.48e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 139 RNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQCLAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLM 218
Cdd:COG4191  31 LLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELE 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 219 NGWIDITERERLARQLREAMRQADEANRAKSV--FLATMSHEIRTPMNAVIGILELVLQRLAPEQRE---RASLEVAYEA 293
Cdd:COG4191 111 ELERDITELERAEEELRELQEQLVQSEKLAALgeLAAGIAHEINNPLAAILGNAELLRRRLEDEPDPeelREALERILEG 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 294 AGSLQLLIGDILDVAKIESGHltltPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLV 373
Cdd:COG4191 191 AERAAEIVRSLRAFSRRDEEE----REPVDLNELIDEALELLRPRLKARGIEVELDLPPDLPP-VLGDPGQLEQVLLNLL 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 374 SNAI---KFTERGQVTIRLQErslDEGRaiVRVDVEDSGIGIAPADQARLFQPFIqvakgrT---VQGGTGLGLAICRKL 447
Cdd:COG4191 266 INAIdamEEGEGGRITISTRR---EGDY--VVISVRDNGPGIPPEVLERIFEPFF------TtkpVGKGTGLGLSISYGI 334

                       330       340
                ....*....|....*....|....
gi 15598240 448 VDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG4191 335 VEKHGGRIEVESEPGGGTTFTITL 358

NtrY

COG5000

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...

101-471

2.39e-43

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: 162.05 E-value: 2.39e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 101 QRTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLtdSDWVEGSKARLMHQQCLAVAR 180
Cdd:COG5000  79 KEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPL--EELLPELDLAELLREALERGW 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 181 GGTASFTdmavRIGGQLLEIHhwVTPYRDRqGRVLGLmngwIDITE---RERLArqlreAMRQadeanraksvFLATMSH 257
Cdd:COG5000 157 QEEIELT----RDGRRTLLVR--ASPLRDD-GYVIVF----DDITEllrAERLA-----AWGE----------LARRIAH 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 258 EIRTPMNAVIGILELVLQRLAPEQRE-----RASLEVAYEAAGSLQLLIGDILDVAKIEsghlTLTPERVRLRHVVESVR 332
Cdd:COG5000 211 EIKNPLTPIQLSAERLRRKLADKLEEdredlERALDTIIRQVDRLKRIVDEFLDFARLP----EPQLEPVDLNELLREVL 286

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 333 RMFEGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIKFTE-RGQVTIRLqerSLDEGRaiVRVDVEDSGIG 411
Cdd:COG5000 287 ALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIEeGGEIEVST---RREDGR--VRIEVSDNGPG 360

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 412 IAPADQARLFQPFIQvakgrTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG5000 361 IPEEVLERIFEPFFT-----TKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRL 415

KinE

COG5809

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...

117-475

1.11e-42

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: 161.68 E-value: 1.11e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 117 LVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTD-SDWVEGSKARLMHQQCLAvaRGGTASFTDMAVRIGG 195
Cdd:COG5809 146 IFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILElIHSDDQENVAAFISQLLK--DGGIAQGEVRFWTKDG 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 196 QLLEIHHWVTPYrDRQGRVLGLMNGWIDITERerlaRQLREAMRQADEANRAkSVFLATMSHEIRTPMNAVIGILELVLQ 275
Cdd:COG5809 224 RWRLLEASGAPI-KKNGEVDGIVIIFRDITER----KKLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKD 297

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 276 RLAPEQRERasLEVAYEAAGSLQLLIGDILDVAKIESGHltltPERVRLRHVVESVRRMFEGLARQKGLRLVVEL-DDAP 354
Cdd:COG5809 298 TIDEEQKTY--LDIMLSELDRIESIISEFLVLAKPQAIK----YEPKDLNTLIEEVIPLLQPQALLKNVQIELELeDDIP 371

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 355 grDVLIDPLRFKQVLSNLVSNAIKFTERGqVTIRLQERSLDEGraIVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQ 434
Cdd:COG5809 372 --DILGDENQLKQVFINLLKNAIEAMPEG-GNITIETKAEDDD--KVVISVTDEGCGIPEERLKKLGEPFYT-----TKE 441

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 15598240 435 GGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLRQ 475
Cdd:COG5809 442 KGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKL 482

phoR_proteo

TIGR02966

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...

196-468

2.84e-42

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: 156.60 E-value: 2.84e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   196 QLLEIHhwVTPYRDrqGRVLGLMNgwiDITERERLarqlrEAMRQAdeanraksvFLATMSHEIRTPMNAVIGILELVLQ 275
Cdd:TIGR02966  83 RVLEIR--IAPYGE--EQKLLVAR---DVTRLRRL-----EQMRRD---------FVANVSHELRTPLTVLRGYLETLAD 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   276 --RLAPEQRERAsLEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDda 353
Cdd:TIGR02966 142 gpDEDPEEWNRA-LEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEALSQGKNHQITFEID-- 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   354 PGRDVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQErslDEGRAivRVDVEDSGIGIAPADQARLFQPFIQVAKGRT 432
Cdd:TIGR02966 219 GGVDVLGDEDELRSAFSNLVSNAIKYTpEGGTITVRWRR---DGGGA--EFSVTDTGIGIAPEHLPRLTERFYRVDKSRS 293

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 15598240   433 VQ-GGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVS 468
Cdd:TIGR02966 294 RDtGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFS 330

REC_hyHK_CKI1_RcsC-like

cd17546

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...

500-614

3.11e-39

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: 140.68 E-value: 3.11e-39

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCERRAPILILg 579
Cdd:cd17546   1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGGRRTPIIAL- 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYL 614
Cdd:cd17546  80 -TANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113

HATPase_c

smart00387

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

360-474

5.15e-37

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

Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 134.31 E-value: 5.15e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240    360 IDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSLDegraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTG 438
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGDH-----VEITVEDNGPGIPPEDLEKIFEPFFRTDKRSRKIGGTG 75

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 15598240    439 LGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLR 474
Cdd:smart00387  76 LGLSIVKKLVELHGGEISVESEPGGGTTFTITLPLE 111

CheY

COG0784

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...

494-623

2.03e-34

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: 127.66 E-value: 2.03e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 494 PSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCERRA 573
Cdd:COG0784   2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIR-ALPRLPDI 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 15598240 574 PILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGRDAA 623
Cdd:COG0784  81 PIIAL--TAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128

HATPase_c

pfam02518

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...

361-475

8.36e-32

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: 119.40 E-value: 8.36e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   361 DPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERsldegrAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRtvQGGTGL 439
Cdd:pfam02518   2 DELRLRQVLSNLLDNALKHAaKAGEITVTLSEG------GELTLTVEDNGIGIPPEDLPRIFEPFSTADKRG--GGGTGL 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15598240   440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLLLRQ 475
Cdd:pfam02518  74 GLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109

KinB

COG5806

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...

224-471

2.65e-30

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: 124.21 E-value: 2.65e-30

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 224 ITERERLARQLREAMRQADEANRAkSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLIGD 303
Cdd:COG5806 178 LIENLIENILLRKELQRAEKLEVV-SELAASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITD 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 304 ILDVAKIESGHLtltpERVRLRHVVESVRRMFEGLARQKGLRLVVELDdaPGRDVLIDPLRFKQVLSNLVSNAIKFTERG 383
Cdd:COG5806 257 YLTFAKPQPEKL----EKIDVSEELEHVIDVLSPYANMNNVEIQTELE--PGLYIEGDRQKLQQCLINIIKNGIEAMPNG 330

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 384 ---QVTIRLQERSldegraiVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLGLAICRKLVDLMGGDVEMHSE 460
Cdd:COG5806 331 gtlTIDVSIDKNK-------VIISIKDTGVGMTKEQLERLGEPYFS-----TKEKGTGLGTMVSYRIIEAMNGTIRVESE 398

                       250
                ....*....|.
gi 15598240 461 PGKGTRVSLDL 471
Cdd:COG5806 399 VGKGTTFTITL 409

cztS_silS_copS

TIGR01386

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...

225-472

7.99e-30

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: 123.65 E-value: 7.99e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   225 TERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLIGDI 304
Cdd:TIGR01386 218 AELRELAQSFNAMLGRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDM 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   305 LDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDApgrdVLIDPLRFKQVLSNLVSNAIKFTERGQ 384
Cdd:TIGR01386 298 LFLARADNGQLALERVRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGL----VRGDPQMFRRAISNLLSNALRHTPDGG 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   385 -VTIRLQERSldegrAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQG-GTGLGLAICRKLVDLMGGDVEMHSEPG 462
Cdd:TIGR01386 374 tITVRIERRS-----DEVRVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGeGTGLGLAIVRSIMEAHGGRASAESPDG 448

                         250
                  ....*....|
gi 15598240   463 KgTRVSLDLL 472
Cdd:TIGR01386 449 K-TRFILRFP 457

PRK11360

two-component system sensor histidine kinase AtoS;

208-471

3.99e-29

two-component system sensor histidine kinase AtoS;

Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 123.15 E-value: 3.99e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  208 RDRQGRVLGLMNGWIDITERERLARQLREAMRQAdeanrAKSVFLATMSHEIRTPMNAVIGILELvLQRLAPEQRERASL 287
Cdd:PRK11360 355 HNTHGEMIGALVIFSDLTERKRLQRRVARQERLA-----ALGELVAGVAHEIRNPLTAIRGYVQI-WRQQTSDPPSQEYL 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  288 EVAYEAAGSLQLLIGDILDVAKieSGHLTLTPerVRLRHVVESVRRMFEGLARQKGLRLVVELD-DAPGrdVLIDPLRFK 366
Cdd:PRK11360 429 SVVLREVDRLNKVIDQLLEFSR--PRESQWQP--VSLNALVEEVLQLFQTAGVQARVDFETELDnELPP--IWADPELLK 502

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  367 QVLSNLVSNAIK-FTERGQVTIRLQERSLDEgraiVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLGLAICR 445
Cdd:PRK11360 503 QVLLNILINAVQaISARGKIRIRTWQYSDGQ----VAVSIEDNGCGIDPELLKKIFDPFFT-----TKAKGTGLGLALSQ 573

                        250       260
                 ....*....|....*....|....*.
gi 15598240  446 KLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:PRK11360 574 RIINAHGGDIEVESEPGVGTTFTLYL 599

PleD

COG3706

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...

497-611

3.02e-28

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: 111.92 E-value: 3.02e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 497 RLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeRRAPIL 576
Cdd:COG3706   1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRT-ADIPII 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 577 ILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:COG3706  80 FL--TALDDEEDRARALEAGADDYLTKPFDPEELL 112

RpfG

COG3437

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...

492-634

2.83e-27

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: 110.64 E-value: 2.83e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 492 MEPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeR 571
Cdd:COG3437   1 MRTGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPST-R 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598240 572 RAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGRDAAQPRGLYDAAAL 634
Cdd:COG3437  80 DIPVIFL--TALADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYL 140

PRK11100

sensory histidine kinase CreC; Provisional

254-471

6.86e-27

sensory histidine kinase CreC; Provisional

Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 114.94 E-value: 6.86e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  254 TMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAgSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRR 333
Cdd:PRK11100 262 TLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSA-RLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  334 MFEGLARQKGLRLVVELDDApgrDVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQersLDEGRaiVRVDVEDSGIGI 412
Cdd:PRK11100 341 AREAQAAAKGITLRLRPDDA---RVLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAE---VDGEQ--VALSVEDQGPGI 412

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15598240  413 APADQARLFQPFIQVAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:PRK11100 413 PDYALPRIFERFYSLPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTL 471

Response_reg

pfam00072

Response regulator receiver domain; This domain receives the signal from the sensor partner in ...

500-615

2.89e-26

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: 103.77 E-value: 2.89e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILILg 579
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIR---RRDPTTPVIIL- 76

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15598240   580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA 615
Cdd:pfam00072  77 -TAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111

BaeS_SmeS

NF012163

sensor histidine kinase efflux regulator BaeS;

226-471

2.00e-25

sensor histidine kinase efflux regulator BaeS;

Pssm-ID: 411086 [Multi-domain] Cd Length: 457 Bit Score: 110.30 E-value: 2.00e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELV---LQRLAPEQRERASLEVayeaaGSLQLLIG 302
Cdd:NF012163 218 ELGKLAQDFNQLASTLEKNEQMRRDFMADISHELRTPLAVLRAELEAIqdgIRKFTPESLDSLQAEV-----GTLTKLVD 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  303 DILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPgrDVLIDPLRFKQVLSNLVSNAIKFTER 382
Cdd:NF012163 293 DLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDS 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  383 GQvTIRLQERSLDEGraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGLGLAICRKLVDLMGGDVEMHSEP 461
Cdd:NF012163 371 GG-SLHISASQRPKE---VTLTVADSAPGVSDEQLARLFERFYRVEVSRNrASGGSGLGLAISLNIVQAHGGTLHAAHSP 446

                        250
                 ....*....|
gi 15598240  462 GKGTRVSLDL 471
Cdd:NF012163 447 LGGLRIVVTL 456

OmpR

COG0745

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...

497-611

5.49e-25

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: 103.11 E-value: 5.49e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 497 RLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPIL 576
Cdd:COG0745   1 MPRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLR---ARPSDIPII 77

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 577 ILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:COG0745  78 ML--TARDDEEDRVRGLEAGADDYLTKPFDPEELL 110

MtrAB_MtrB

NF040691

MtrAB system histidine kinase MtrB;

230-471

1.09e-24

MtrAB system histidine kinase MtrB;

Pssm-ID: 468655 [Multi-domain] Cd Length: 507 Bit Score: 108.57 E-value: 1.09e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  230 LARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVigilelvlqRLAPE----QRE------RASLEVAYEAAGSLQL 299
Cdd:NF040691 253 MADSLQRQIRQLEELSRLQQRFVSDVSHELRTPLTTI---------RMAADvihdSRDdfdpatARSAELLHTELDRFES 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  300 LIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGrDVLIDPLRFKQVLSNLVSNAIKF 379
Cdd:NF040691 324 LLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVELRVDAPGTPV-VAEVDPRRVERVLRNLVVNAIEH 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  380 TERGQVTIRlqersLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQV--AKGRTVqGGTGLGLAICRKLVDLMGGDVEM 457
Cdd:NF040691 403 GEGKPVVVT-----VAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdpARARTT-GGTGLGLAIALEDARLHGGWLEA 476

                        250
                 ....*....|....
gi 15598240  458 HSEPGKGTRVSLDL 471
Cdd:NF040691 477 WGRPGQGSQFRLTL 490

PRK13837

two-component system VirA-like sensor kinase;

225-626

2.53e-23

two-component system VirA-like sensor kinase;

Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 105.92 E-value: 2.53e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  225 TERERLARQLREAMRQadeanRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLIGDI 304
Cdd:PRK13837 432 TERDALERRLEHARRL-----EAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQI 506

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  305 LDVAKieSGHLTLTPERV-RLRHVVESVRRMfeglARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAIK-FTER 382
Cdd:PRK13837 507 LAFGR--KGERNTKPFDLsELVTEIAPLLRV----SLPPGVELDFDQDQEPAV-VEGNPAELQQVLMNLCSNAAQaMDGA 579

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  383 GQVTIRLQERSLDEGRA----------IVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLGLAICRKLVDLMG 452
Cdd:PRK13837 580 GRVDISLSRAKLRAPKVlshgvlppgrYVLLRVSDTGAGIDEAVLPHIFEPFFT-----TRAGGTGLGLATVHGIVSAHA 654

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  453 GDVEMHSEPGKGTRVSLDLLLRQCGPKMPESGQDPLAASMepSRRLHILIADDYPPNRVLLRQQLEFLGH------RVAE 526
Cdd:PRK13837 655 GYIDVQSTVGRGTRFDVYLPPSSKVPVAPQAFFGPGPLPR--GRGETVLLVEPDDATLERYEEKLAALGYepvgfsTLAA 732

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  527 AedgqVALELWADERFEVLISDcnMPRLNGYQLARRIRIQERCerrAPILILGytaDAEPDEVQRCRDAGMDDCLFKPLG 606
Cdd:PRK13837 733 A----IAWISKGPERFDLVLVD--DRLLDEEQAAAALHAAAPT---LPIILGG---NSKTMALSPDLLASVAEILAKPIS 800

                        410       420
                 ....*....|....*....|
gi 15598240  607 LETLRNYLATSFGRDAAQPR 626
Cdd:PRK13837 801 SRTLAYALRTALATARAAAA 820

phoR

PRK11006

phosphate regulon sensor histidine kinase PhoR;

225-474

3.53e-23

phosphate regulon sensor histidine kinase PhoR;

Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 103.17 E-value: 3.53e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  225 TERERL--ARQLREaMRQADEANRAksvFLATMSHEIRTPMNAVIGILELVL-QRLAPEQRERAsLEVAYEAAGSLQLLI 301
Cdd:PRK11006 183 TEGQLLmvARDVTQ-MHQLEGARRN---FFANVSHELRTPLTVLQGYLEMMQdQPLEGALREKA-LHTMREQTQRMEGLV 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  302 GDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGlRLVVELDdaPGRDVLIDPLRFKQVLSNLVSNAIKFTE 381
Cdd:PRK11006 258 KQLLTLSKIEAAPTIDLNEKVDVPMMLRVLEREAQTLSQGKH-TITFEVD--NSLKVFGNEDQLRSAISNLVYNAVNHTP 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  382 RG-QVTIRLQERSldEGraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAICRKLVDLMGGDVEMHS 459
Cdd:PRK11006 335 EGtHITVRWQRVP--QG---AEFSVEDNGPGIAPEHIPRLTERFYRVDKARSRQtGGSGLGLAIVKHALSHHDSRLEIES 409

                        250
                 ....*....|....*
gi 15598240  460 EPGKGTRVSLDLLLR 474
Cdd:PRK11006 410 EVGKGTRFSFVLPER 424

PRK13557

histidine kinase; Provisional

204-584

4.84e-23

histidine kinase; Provisional

Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 103.60 E-value: 4.84e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  204 VTPYRDRQGRVLGLMNGWIDITERerlaRQLREAMRQADEAnRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPE--- 280
Cdd:PRK13557 124 VSPVYNDAGDLVYFFGSQLDVSRR----RDAEDALRQAQKM-EALGQLTGGIAHDFNNLLQVMSGYLDVIQAALSHPdad 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  281 -QRERASLEVAYEAAGSLQLLIGDILDVAKIESghltLTPERVRLRHVVESVRRMFEglaRQKGLRLVVELDDAPG-RDV 358
Cdd:PRK13557 199 rGRMARSVENIRAAAERAATLTQQLLAFARKQR----LEGRVLNLNGLVSGMGELAE---RTLGDAVTIETDLAPDlWNC 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  359 LIDPLRFKQVLSNLVSNAIK-FTERGQVTIRLQERSLDE-----------GRaIVRVDVEDSGIGIAPADQARLFQPFIq 426
Cdd:PRK13557 272 RIDPTQAEVALLNVLINARDaMPEGGRVTIRTRNVEIEDedlamyhglppGR-YVSIAVTDTGSGMPPEILARVMDPFF- 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  427 vakgrTVQG---GTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDLllrqcgPKMPESGQDPLAASMEPSRRL---HI 500
Cdd:PRK13557 350 -----TTKEegkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYF------PASDQAENPEQEPKARAIDRGgteTI 418

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  501 LIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADE-RFEVLISDCNMP-RLNGYQLARRIRiqerceRRAP---- 574
Cdd:PRK13557 419 LIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAREAR------RRQPkikv 492

                        410
                 ....*....|
gi 15598240  575 ILILGYtADA 584
Cdd:PRK13557 493 LLTTGY-AEA 501

REC

cd00156

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...

501-604

1.90e-22

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: 92.29 E-value: 1.90e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 501 LIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILILgy 580
Cdd:cd00156   1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLR---ELPPDIPVIVL-- 75

                        90       100
                ....*....|....*....|....
gi 15598240 581 TADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd00156  76 TAKADEEDAVRALELGADDYLVKP 99

PRK10364

two-component system sensor histidine kinase ZraS;

226-471

4.01e-22

two-component system sensor histidine kinase ZraS;

Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 100.25 E-value: 4.01e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLIGDIL 305
Cdd:PRK10364 215 RRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  306 DVAKieSGHLTLTPerVRLRHVVESVRRMFEGLARQKGLRLvvELDDAPGRDVL-IDPLRFKQVLSNLVSNAIK-FTERG 383
Cdd:PRK10364 295 ELVK--PTHLALQA--VDLNDLINHSLQLVSQDANSREIQL--RFTANDTLPEIqADPDRLTQVLLNLYLNAIQaIGQHG 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  384 QVTIrlqerSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGK 463
Cdd:PRK10364 369 VISV-----TASESGAGVKISVTDSGKGIAADQLEAIFTPYFT-----TKAEGTGLGLAVVHNIVEQHGGTIQVASQEGK 438


                 ....*...
gi 15598240  464 GTRVSLDL 471
Cdd:PRK10364 439 GATFTLWL 446

PRK09835

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

226-471

7.15e-22

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

Pssm-ID: 182101 [Multi-domain] Cd Length: 482 Bit Score: 99.46 E-value: 7.15e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQrlapEQRERASLE-VAY---EAAGSLQLLI 301
Cdd:PRK09835 240 ELEQLVLSFNHMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALS----QSRSQKELEdVLYsnlEELTRMAKMV 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  302 GDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVElddapGRDVLI--DPLRFKQVLSNLVSNAIKF 379
Cdd:PRK09835 316 SDMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELRFV-----GDPCQVagDPLMLRRAISNLLSNALRY 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  380 TERGQ-VTIRLQERSldegrAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQG-GTGLGLAICRKLVDLMGGDVEM 457
Cdd:PRK09835 391 TPAGEaITVRCQEVD-----HQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGeGSGIGLAIVKSIVVAHKGTVAV 465

                        250
                 ....*....|....
gi 15598240  458 HSEPgKGTRVSLDL 471
Cdd:PRK09835 466 TSDA-RGTRFVISL 478

KinA

COG5805

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...

204-471

2.82e-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: 97.88 E-value: 2.82e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 204 VTPYRDRQGRVLGLMngWI--DITERerlaRQLREAMRQADEANRAKSVfLATMSHEIRTPMNAVIGILELvLQRLAPEQ 281
Cdd:COG5805 248 IVPLIDTDGSVKGIL--VIlrDITEK----KEAEELMARSEKLSIAGQL-AAGIAHEIRNPLTSIKGFLQL-LQPGIEDK 319

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 282 REraSLEVAYEAAGSLQLLIGDILDVAKIESGHLtltpERVRLRHVVESVRRMFEGLARQKGLRLVVELDDaPGRDVLID 361
Cdd:COG5805 320 EE--YFDIMLSELDRIESIISEFLALAKPQAVNK----EKENINELIQDVVTLLETEAILHNIQIRLELLD-EDPFIYCD 392

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 362 PLRFKQVLSNLVSNAIKFTERGQvTIRLQERSLDEGraiVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLGL 441
Cdd:COG5805 393 ENQIKQVFINLIKNAIEAMPNGG-TITIHTEEEDNS---VIIRVIDEGIGIPEERLKKLGEPFFT-----TKEKGTGLGL 463

                       250       260       270
                ....*....|....*....|....*....|
gi 15598240 442 AICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG5805 464 MVSYKIIENHNGTIDIDSKVGKGTTFTITL 493

CitA

COG3290

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...

102-471

3.39e-21

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

Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 96.46 E-value: 3.39e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRnylESLRMTREQARGTLLTDsdwvegskarlmhqQCLAVARG 181
Cdd:COG3290  74 KLLEEIARLVEEREAVLESIREGVIAVDRDGRITLIND---AARRLLGLDAIGRPIDE--------------VLAEVLET 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 182 GTasfTDMAVRIGGQLLEIHhwVTPYRDRqGRVLGLMNGWIDITERERLARQLrEAMRQADEANRAksvflatMSHEIRT 261
Cdd:COG3290 137 GE---RDEEILLNGRVLVVN--RVPIRDD-GRVVGAVATFRDRTELERLEEEL-EGVKELAEALRA-------QRHDFRN 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 262 PMNAVIGILELvlqrlapEQRERAsLEVAYEAAGSLQLLIGDILDvaKIESghltltpervrlrHVVESVRRMFEGLARQ 341
Cdd:COG3290 203 HLHTISGLLQL-------GEYDEA-LEYIDEISEELQELIDSLLS--RIGN-------------PVLAALLLGKAARARE 259

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 342 KGLRLVVELDDAPgRDVLIDPLRFKQVLSNLVSNAI-----KFTERGQVTIRLQErslDEGRAIVRVdvEDSGIGIAPAD 416
Cdd:COG3290 260 RGIDLTIDIDSDL-PDLPLSDTDLVTILGNLLDNAIeavekLPEEERRVELSIRD---DGDELVIEV--EDSGPGIPEEL 333

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240 417 QARLFQpfiqvaKGRT--VQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:COG3290 334 LEKIFE------RGFStkLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVRL 384

HATPase_BaeS-like

cd16946

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

361-471

6.71e-21

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: 88.29 E-value: 6.71e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFTERGQvTIRLQERSLDEGraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGL 439
Cdd:cd16946   1 DRDRLQQLFVNLLENSLRYTDTGG-KLRIRAAQTPQE---VRLDVEDSAPGVSDDQLARLFERFYRVESSRNrASGGSGL 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16946  77 GLAICHNIALAHGGTISAEHSPLGGLRLVLTL 108

PRK10490

sensor protein KdpD; Provisional

226-471

1.70e-20

sensor protein KdpD; Provisional

Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 97.03 E-value: 1.70e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQlREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERA-SLEVAYEAAGSLQLLIGDI 304
Cdd:PRK10490 643 ERLTLTAS-EEQARLASEREQLRNALLAALSHDLRTPLTVLFGQAEILTLDLASEGSPHArQASEIRQQVLNTTRLVNNL 721

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  305 LDVAKIESGHLTLTPERVRLRHVVESVRRMFE-GLARQKglrlvVELDdAPGRDVLI--DPLRFKQVLSNLVSNAIKFT- 380
Cdd:PRK10490 722 LDMARIQSGGFNLRKEWLTLEEVVGSALQMLEpGLSGHP-----INLS-LPEPLTLIhvDGPLFERVLINLLENAVKYAg 795

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  381 ERGQVTIRLQErsldEGRAIvRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGgTGLGLAICRKLVDLMGGDVEMHSE 460
Cdd:PRK10490 796 AQAEIGIDAHV----EGERL-QLDVWDNGPGIPPGQEQLIFDKFARGNKESAIPG-VGLGLAICRAIVEVHGGTIWAENR 869

                        250
                 ....*....|...
gi 15598240  461 PGKGT--RVSLDL 471
Cdd:PRK10490 870 PEGGAcfRVTLPL 882

HATPase_AtoS-like

cd16943

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

362-471

4.83e-20

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: 85.55 E-value: 4.83e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 362 PLRFKQVLSNLVSNAIK-FTERGQVTIRLqerSLDEGRAIVrvDVEDSGIGIAPADQARLFQPFIQVakgRTVQGGTGLG 440
Cdd:cd16943   1 PSQLNQVLLNLLVNAAQaMEGRGRITIRT---WAHVDQVLI--EVEDTGSGIDPEILGRIFDPFFTT---KPVGEGTGLG 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 441 LAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16943  73 LSLSYRIIQKHGGTIRVASVPGGGTRFTIIL 103

YesN

COG4753

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...

500-604

1.06e-19

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: 84.44 E-value: 1.06e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILI 577
Cdd:COG4753   2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIR---ELDPDTKIII 78

                        90       100
                ....*....|....*....|....*..
gi 15598240 578 LgyTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:COG4753  79 L--SGYSDFEYAQEAIKLGADDYLLKP 103

REC_2_DhkD-like

cd17580

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...

500-614

1.98e-19

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: 84.05 E-value: 1.98e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCErRAPILILg 579
Cdd:cd17580   1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLA-NTPAIAL- 78

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYL 614
Cdd:cd17580  79 -TGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112

PRK09303

histidine kinase;

226-464

9.17e-19

histidine kinase;

Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 88.85 E-value: 9.17e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  226 ERERLARQLReamrqadeanrAKSVFLATMSHEIRTPMNA-VIGI--LELVLQR----LAPEQRERAsLEVAYEAAGSLQ 298
Cdd:PRK09303 140 ENETLLEQLK-----------FKDRVLAMLAHDLRTPLTAaSLALetLELGQIDedteLKPALIEQL-QDQARRQLEEIE 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  299 LLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVEL-DDAPgrDVLIDPLRFKQVLSNLVSNAI 377
Cdd:PRK09303 208 RLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQTDIpSDLP--SVYADQERIRQVLLNLLDNAI 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  378 KFT-ERGQVTIRLQERSLDEgraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTvQGGTGLGLAICRKLVDLMGGDVE 456
Cdd:PRK09303 286 KYTpEGGTITLSMLHRTTQK----VQVSICDTGPGIPEEEQERIFEDRVRLPRDEG-TEGYGIGLSVCRRIVRVHYGQIW 360


                 ....*...
gi 15598240  457 MHSEPGKG 464
Cdd:PRK09303 361 VDSEPGQG 368

AtoC

COG2204

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...

496-624

1.02e-17

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];

Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 86.17 E-value: 1.02e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 496 RRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCErrAPI 575
Cdd:COG2204   1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR-ALDPD--LPV 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15598240 576 LILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGRDAAQ 624
Cdd:COG2204  78 ILL--TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRRLR 124

envZ

PRK09467

osmolarity sensor protein; Provisional

233-471

1.55e-17

osmolarity sensor protein; Provisional

Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 85.73 E-value: 1.55e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  233 QLREAMRQAdEANRAksVFLATMSHEIRTPMNAVigilelvlqRLAPEQrerASLEVAYEAAGslqlLIGDILDVAKIES 312
Cdd:PRK09467 217 QMAAGIKQL-EDDRT--LLMAGVSHDLRTPLTRI---------RLATEM---MSEEDGYLAES----INKDIEECNAIIE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  313 GHLTLtpervrLRHVVESVRRMF-------EGLARQKGLRLVVELDDAPG-RDVLIDPLRFKQVLSNLVSNAIKFTeRGQ 384
Cdd:PRK09467 278 QFIDY------LRTGQEMPMEMAdlnallgEVIAAESGYEREIETALQPGpIEVPMNPIAIKRALANLVVNAARYG-NGW 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  385 VTIRlqerSLDEGRAiVRVDVEDSGIGIAPADQARLFQPFIQvakGRTVQG--GTGLGLAICRKLVDLMGGDVEM--HSE 460
Cdd:PRK09467 351 IKVS----SGTEGKR-AWFQVEDDGPGIPPEQLKHLFQPFTR---GDSARGssGTGLGLAIVKRIVDQHNGKVELgnSEE 422

                        250
                 ....*....|.
gi 15598240  461 PGKGTRVSLDL 471
Cdd:PRK09467 423 GGLSARAWLPL 433

HATPase_EcPhoR-like

cd16952

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

369-468

2.04e-17

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: 78.40 E-value: 2.04e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 369 LSNLVSNAIKFT-ERGQVTIRLQErslDEGRAivRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAICRK 446
Cdd:cd16952   5 FSNLVSNAVKYTpPSDTITVRWSQ---EESGA--RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNtGGTGLGLAIVKH 79

                        90       100
                ....*....|....*....|..
gi 15598240 447 LVDLMGGDVEMHSEPGKGTRVS 468
Cdd:cd16952  80 VMSRHDARLLIASELGKGSRFT 101

HATPase_BceS-YxdK-YvcQ-like

cd16948

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

363-469

2.56e-17

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: 78.10 E-value: 2.56e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 363 LRFkqVLSNLVSNAIKFT-ERGQVTIRLQErslDEGRaiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGLGL 441
Cdd:cd16948   6 LSF--IIGQIVSNALKYSkQGGKIEIYSET---NEQG--VVLSIKDFGIGIPEEDLPRVFDKGFTGENGRNFQESTGMGL 78

                        90       100
                ....*....|....*....|....*...
gi 15598240 442 AICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:cd16948  79 YLVKKLCDKLGHKIDVESEVGEGTTFTI 106

HATPase_EnvZ-like

cd16950

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

366-470

4.06e-17

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: 77.10 E-value: 4.06e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 366 KQVLSNLVSNAIKFTeRGQVtirlqERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVqGGTGLGLAICR 445
Cdd:cd16950   2 KRVLSNLVDNALRYG-GGWV-----EVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGT-SGTGLGLAIVQ 74

                        90       100
                ....*....|....*....|....*..
gi 15598240 446 KLVDLMGGDVEMHSEPGKG--TRVSLD 470
Cdd:cd16950  75 RISDAHGGSLTLANRAGGGlcARIELP 101

REC_OmpR

cd17574

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...

501-604

4.50e-17

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

Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 77.06 E-value: 4.50e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 501 LIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPILILgy 580
Cdd:cd17574   1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREK---GSDIPIIML-- 75

                        90       100
                ....*....|....*....|....*
gi 15598240 581 TA-DAEPDEVqRCRDAGMDDCLFKP 604
Cdd:cd17574  76 TAkDEEEDKV-LGLELGADDYITKP 99

REC_OmpR_PhoB

cd17618

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...

499-604

6.08e-17

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: 77.29 E-value: 6.08e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeRRAPILIL 578
Cdd:cd17618   2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMT-RDIPIIML 80

                        90       100
                ....*....|....*....|....*.
gi 15598240 579 gyTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17618  81 --TARGEEEDKVRGLEAGADDYITKP 104

PEP_his_kin

TIGR02916

putative PEP-CTERM system histidine kinase; Members of this protein family have a novel ...

318-471

6.92e-17

putative PEP-CTERM system histidine kinase; Members of this protein family have a novel N-terminal domain, a single predicted membrane-spanning helix, and a predicted cystosolic histidine kinase domain. We designate this protein PrsK, and its companion DNA-binding response regulator protein (TIGR02915) PrsR. These predicted signal-transducing proteins appear to enable enhancer-dependent transcriptional activation. The prsK gene is often associated with exopolysaccharide biosynthesis genes. [Protein fate, Protein and peptide secretion and trafficking, Signal transduction, Two-component systems]

Pssm-ID: 274349 [Multi-domain] Cd Length: 679 Bit Score: 84.77 E-value: 6.92e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   318 TPERVRLRHVVESVRRMFEGlARQKGLRLVVELDdaPGRDVLIDPLRFKQVLSNLVSNAIKFTE-RGQVTIRLQERSlde 396
Cdd:TIGR02916 536 LEEEKLCVDLVDLLRRAIAS-KRAQGPRPEVSID--TDLSVRADRERLERVLGHLVQNALEATPgEGRVAIRVEREC--- 609

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240   397 grAIVRVDVEDSGIGIAPA-DQARLFQPFiqvakgRTVQG-GTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:TIGR02916 610 --GAARIEIEDSGCGMSPAfIRERLFKPF------DTTKGaGMGIGVYECRQYVEEIGGRIEVESTPGQGTIFTLVL 678

HATPase_FilI-like

cd16921

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

367-467

7.65e-17

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: 76.60 E-value: 7.65e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 367 QVLSNLVSNAIKFTeRGQVTIRLQERSLDEGRAiVRVDVEDSGIGIAPADQARLFQPFiQVAKGRTVQGGTGLGLAICRK 446
Cdd:cd16921   3 QVLTNLLGNAIKFR-RPRRPPRIEVGAEDVGEE-WTFYVRDNGIGIDPEYAEKVFGIF-QRLHSREEYEGTGVGLAIVRK 79

                        90       100
                ....*....|....*....|.
gi 15598240 447 LVDLMGGDVEMHSEPGKGTRV 467
Cdd:cd16921  80 IIERHGGRIWLESEPGEGTTF 100

glnL

PRK11073

nitrogen regulation protein NR(II);

255-474

8.08e-17

nitrogen regulation protein NR(II);

Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 82.44 E-value: 8.08e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  255 MSHEIRTPMNAVIGILELvLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAK-----IESGHltltpervrlrHVVE 329
Cdd:PRK11073 137 LAHEIKNPLGGLRGAAQL-LSKALPDPALTEYTKVIIEQADRLRNLVDRLLGPQRpgthvTESIH-----------KVAE 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  330 SVRRMFEgLARQKGLRLVVELDDA-PgrDVLIDPLRFKQVLSNLVSNAIKFTERGQVTIRLQERSLDEG-------RAIV 401
Cdd:PRK11073 205 RVVQLVS-LELPDNVRLIRDYDPSlP--ELAHDPDQIEQVLLNIVRNALQALGPEGGTITLRTRTAFQLtlhgeryRLAA 281

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598240  402 RVDVEDSGIGIAPADQARLFQPFIQvakGRtvQGGTGLGLAICRKLVDLMGGDVEMHSEPGKgTRVSLDLLLR 474
Cdd:PRK11073 282 RIDIEDNGPGIPPHLQDTLFYPMVS---GR--EGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFSVYLPIR 348

HATPase_TutC-TodS-like

cd16925

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...

361-471

1.35e-16

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

Pssm-ID: 340402 [Multi-domain] Cd Length: 110 Bit Score: 75.99 E-value: 1.35e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFTERGQVtIRLQERSLDEGRAIVrvDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGL 439
Cdd:cd16925   1 DAEKYERVVLNLLSNAFKFTPDGGR-IRCILEKFRLNRFLL--TVSDSGPGIPPNLREEIFERFRQGDGSSTRAhGGTGL 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16925  78 GLSIVKEFVELHGGTVTVSDAPGGGALFQVEL 109

PRK10549

two-component system sensor histidine kinase BaeS;

229-473

1.87e-16

two-component system sensor histidine kinase BaeS;

Pssm-ID: 182539 [Multi-domain] Cd Length: 466 Bit Score: 82.76 E-value: 1.87e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  229 RLARQLR--EAMRQAdeanraksvFLATMSHEIRTPMNAVIGILELV---LQRLAPEQRERASLEVAyeaagSLQLLIGD 303
Cdd:PRK10549 228 QLASTLEknEQMRRD---------FMADISHELRTPLAVLRGELEAIqdgVRKFTPESVASLQAEVG-----TLTKLVDD 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  304 ILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPgrDVLIDPLRFKQVLSNLVSNAIKFT-ER 382
Cdd:PRK10549 294 LHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSA--TVFGDPDRLMQLFNNLLENSLRYTdSG 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  383 GQVTIRLQERSldegrAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRT-VQGGTGLGLAICRKLVDLMGGDV-EMHSE 460
Cdd:PRK10549 372 GSLHISAEQRD-----KTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNrASGGSGLGLAICLNIVEAHNGRIiAAHSP 446

                        250
                 ....*....|...
gi 15598240  461 PGkGTRVSLDLLL 473
Cdd:PRK10549 447 FG-GVSITVELPL 458

REC_CheY4-like

cd17562

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...

499-610

1.88e-16

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: 75.80 E-value: 1.88e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcERRAPILIL 578
Cdd:cd17562   2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPA-YKFTPILML 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 579 gyTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:cd17562  81 --TTESSDEKKQEGKAAGATGWLVKPFDPEQL 110

HATPase_Glnl-NtrB-like

cd16918

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

367-469

3.92e-16

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: 74.74 E-value: 3.92e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 367 QVLSNLVSNAIKFTERGQVTIRLQER-------SLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQvakGRtvQGGTGL 439
Cdd:cd16918   3 QVFLNLVRNAAQALAGSGGEIILRTRtqrqvtlGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPMVS---GR--ENGTGL 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 440 GLAICRKLVDLMGGDVEMHSEPGKGT-RVSL 469
Cdd:cd16918  78 GLAIAQNIVSQHGGVIECDSQPGHTVfSVSL 108

HATPase_TmoS-FixL-DctS-like

cd16920

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

366-469

4.86e-16

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: 74.36 E-value: 4.86e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 366 KQVLSNLVSNAIK-----FTERGQVTIRLQERSLDEgraiVRVDVEDSGIGIAPADQARLFQPFIQvakgrTVQGGTGLG 440
Cdd:cd16920   2 QQVLINLVRNGIEamsegGCERRELTIRTSPADDRA----VTISVKDTGPGIAEEVAGQLFDPFYT-----TKSEGLGMG 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 441 LAICRKLVDLMGGDVEMHSEPGKGT--RVSL 469
Cdd:cd16920  73 LSICRSIIEAHGGRLSVESPAGGGAtfQFTL 103

PRK10604

sensor protein RstB; Provisional

256-469

8.49e-16

sensor protein RstB; Provisional

Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 80.42 E-value: 8.49e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  256 SHEIRTPMNAVIGILELVLQRLAPEQrerASLEvayEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMF 335
Cdd:PRK10604 220 AHELRTPLVRLRYRLEMSDNLSAAES---QALN---RDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAWLSTHLADI 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  336 EGLARQKglrlVVELDDAPGRDVLI-DPLRFKQVLSNLVSNAIKFTErGQVTIRLqerSLDEGRAIVRVdvEDSGIGIAP 414
Cdd:PRK10604 294 QAVTPEK----TVRLDTPHQGDYGAlDMRLMERVLDNLLNNALRYAH-SRVRVSL---LLDGNQACLIV--EDDGPGIPP 363

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15598240  415 ADQARLFQPFIQVAKGRT-VQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:PRK10604 364 EERERVFEPFVRLDPSRDrATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419

HATPase_BasS-like

cd16940

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

361-471

1.17e-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 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: 73.59 E-value: 1.17e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSldegRAIVRVdvEDSGIGIAPADQARLFQPFIQVAKgrTVQGGTGL 439
Cdd:cd16940  10 DALLLFLLLRNLVDNAVRYSpQGSRVEIKLSADD----GAVIRV--EDNGPGIDEEELEALFERFYRSDG--QNYGGSGL 81

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16940  82 GLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113

REC_D1_PleD-like

cd17538

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...

499-604

1.87e-15

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: 72.53 E-value: 1.87e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcERRAPILIL 578
Cdd:cd17538   1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPE-TRHIPVIMI 79

                        90       100
                ....*....|....*....|....*.
gi 15598240 579 gyTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17538  80 --TALDDREDRIRGLEAGADDFLSKP 103

REC_CheY_CheY3

cd19923

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...

498-611

4.64e-15

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

Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 71.99 E-value: 4.64e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPPNRVLLRQQLEFLGHR-VAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcERRAPIL 576
Cdd:cd19923   1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGA-LSHLPVL 79

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 577 ILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:cd19923  80 MV--TAEAKKENVIAAAQAGVNNYIVKPFTAATLK 112

HATPase_RstB-like

cd16939

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

368-471

6.13e-15

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: 71.31 E-value: 6.13e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIKFTERgqvTIRLQERsLDEGRAivRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAICRK 446
Cdd:cd16939   4 ALDNLLRNALRYAHR---TVRIALL-VSGGRL--TLIVEDDGPGIPAAARERVFEPFVRLDPSRDRAtGGFGLGLAIVHR 77

                        90       100
                ....*....|....*....|....*
gi 15598240 447 LVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16939  78 VALWHGGHVECDDSELGGACFRLTW 102

CitB

COG4565

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...

496-611

1.43e-14

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

Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 71.15 E-value: 1.43e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 496 RRLHILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRA 573
Cdd:COG4565   2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELR---ARGPDV 78

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15598240 574 PILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:COG4565  79 DVIVI--TAARDPETVREALRAGVVDYLIKPFTFERLR 114

REC_ETR-like

cd19933

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...

498-614

2.54e-14

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: 69.74 E-value: 2.54e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADER--FEVLISDCNMPRLNGYQLArrIRIQERCERRAPI 575
Cdd:cd19933   1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVA--LRIRKLFGRRERP 78

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598240 576 LILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYL 614
Cdd:cd19933  79 LIVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117

REC_PA4781-like

cd19920

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...

500-604

4.50e-14

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: 68.69 E-value: 4.50e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcERRAPILILg 579
Cdd:cd19920   1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPA-TRHIPVIFL- 78

                        90       100
                ....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd19920  79 -TALTDTEDKVKGFELGAVDYITKP 102

REC_hyHK

cd17598

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...

500-604

4.82e-14

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

Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 68.89 E-value: 4.82e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeRRAPILILg 579
Cdd:cd17598   1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDL-KDIPVILL- 78

                        90       100
                ....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17598  79 -TTLSDPRDVIRGLECGADNFITKP 102

REC_CheV-like

cd19924

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...

500-604

4.97e-14

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

Pssm-ID: 381151 [Multi-domain] Cd Length: 111 Bit Score: 68.94 E-value: 4.97e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALEL---WADE------RFEVLISDCNMPRLNGYQLARRIRiQERCE 570
Cdd:cd19924   1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKlenLAKEgndlskELDLIITDIEMPKMDGYELTFELR-DDPRL 79

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598240 571 RRAPILILGYTADaePDEVQRCRDAGMDDCLFKP 604
Cdd:cd19924  80 ANIPVILNSSLSG--EFSRARGKKVGADAYLAKF 111

REC_CheC-like

cd17593

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...

498-615

8.86e-14

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: 68.33 E-value: 8.86e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPpnrvLLRQQL-----EFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerr 572
Cdd:cd17593   1 MKVLICDDSS----MARKQLaralpADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQ----- 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15598240 573 APILILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA 615
Cdd:cd17593  72 LETKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLE 114

REC_PdtaR-like

cd19932

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...

498-620

2.02e-13

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

Pssm-ID: 381159 [Multi-domain] Cd Length: 118 Bit Score: 67.44 E-value: 2.02e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPPNRVLLRQQLEFLGHRV-AEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIriqeRCERRAPIL 576
Cdd:cd19932   1 VRVLIAEDEALIRMDLREMLEEAGYEVvGEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKII----TSENIAPIV 76

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15598240 577 ILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGR 620
Cdd:cd19932  77 LL--TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118

REC_DivK-like

cd17548

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...

500-605

2.13e-13

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: 67.18 E-value: 2.13e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCERrapILILG 579
Cdd:cd17548   2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRD---IPVIA 78

                        90       100
                ....*....|....*....|....*.
gi 15598240 580 YTADAEPDEVQRCRDAGMDDCLFKPL 605
Cdd:cd17548  79 LTAYAMKGDREKILEAGCDGYISKPI 104

HisKA

pfam00512

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

247-313

2.37e-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: 65.31 E-value: 2.37e-13

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240   247 AKSVFLATMSHEIRTPMNAVIGILELvLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAKIESG 313
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLEL-LRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66

PRK10618

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

227-488

2.48e-13

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

Pssm-ID: 236726 [Multi-domain] Cd Length: 894 Bit Score: 73.81 E-value: 2.48e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  227 RERL-ARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELvLQRLAPEQRERASLEVAYEAAGSLQLLIGDIL 305
Cdd:PRK10618 428 REVLvNKKLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQ-LRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQ 506

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  306 DVAKIESGHLTLTPERVRLRHVVESVrrMFEGLA--RQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTERG 383
Cdd:PRK10618 507 LLNMLETQDWKPEQELFSLQDLIDEV--LPEVLPaiKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYG 584

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  384 QVTIRLqerSLDEGRA-IVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPG 462
Cdd:PRK10618 585 KITLEV---DQDESSPdRLTIRILDTGAGVSIKELDNLHFPFLNQTQGDRYGKASGLTFFLCNQLCRKLGGHLTIKSREG 661

                        250       260
                 ....*....|....*....|....*.
gi 15598240  463 KGTRVSLDLLLrQCGPKMPESGQDPL 488
Cdd:PRK10618 662 LGTRYSIHLKM-LAADPEVEEEEEKL 686

REC_OmpR_PrrA-like

cd17627

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...

500-610

5.03e-13

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381142 [Multi-domain] Cd Length: 116 Bit Score: 66.25 E-value: 5.03e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILILg 579
Cdd:cd17627   1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLR---AAGNDLPILVL- 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:cd17627  77 -TARDSVSDRVAGLDAGADDYLVKPFALEEL 106

REC_OmpR_KdpE-like

cd17620

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...

500-604

6.24e-13

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: 65.26 E-value: 6.24e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerRAPILILg 579
Cdd:cd17620   1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWS----AVPVIVL- 75

                        90       100
                ....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17620  76 -SARDEESDKIAALDAGADDYLTKP 99

HisKA

smart00388

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

247-313

8.20e-13

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

Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 63.74 E-value: 8.20e-13

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240    247 AKSVFLATMSHEIRTPMNAVIGILELvLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAKIESG 313
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLEL-LLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66

HATPase_HupT_MifS-like

cd16976

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

367-471

1.03e-12

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: 64.79 E-value: 1.03e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 367 QVLSNLVSNAIKFTERGQV-TIRLQERSLDeGRAIVRVdvEDSGIGIAPADQARLFQPFIQVakgRTVQGGTGLGLAICR 445
Cdd:cd16976   3 QVLMNLLQNALDAMGKVENpRIRIAARRLG-GRLVLVV--RDNGPGIAEEHLSRVFDPFFTT---KPVGKGTGLGLSISY 76

                        90       100
                ....*....|....*....|....*.
gi 15598240 446 KLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16976  77 GIVEEHGGRLSVANEEGAGARFTFDL 102

HisKA

cd00082

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...

245-309

1.20e-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: 63.39 E-value: 1.20e-12

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598240 245 NRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAK 309
Cdd:cd00082   1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65

HATPase_CreC-like

cd16945

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

361-464

1.22e-12

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: 64.79 E-value: 1.22e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFTERGQvTIRLQERSLDEGraiVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGLG 440
Cdd:cd16945   1 DPFLLRQAINNLLDNAIDFSPEGG-LIALQLEADTEG---IELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKSTGLG 76

                        90       100
                ....*....|....*....|....
gi 15598240 441 LAICRKLVDLMGGDVEMHSEPGKG 464
Cdd:cd16945  77 LAFVQEVAQLHGGRITLRNRPDGV 100

REC_NarL-like

cd17535

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...

500-596

1.43e-12

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: 64.84 E-value: 1.43e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNR----VLLRQQLEFlgHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPI 575
Cdd:cd17535   1 VLIVDDHPLVReglrRLLESEPDI--EVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLR---RRYPDLKV 75

                        90       100
                ....*....|....*....|.
gi 15598240 576 LILgyTADAEPDEVQRCRDAG 596
Cdd:cd17535  76 IVL--TAHDDPEYVLRALKAG 94

REC_2_GGDEF

cd17544

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...

499-604

1.79e-12

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: 64.46 E-value: 1.79e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADER-FEVLISDCNMPRLNGYQLARRIRIQERCERRApilI 577
Cdd:cd17544   2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLA---I 78

                        90       100
                ....*....|....*....|....*..
gi 15598240 578 LGYTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17544  79 IGISASGDNALSARFIKAGANDFLTKP 105

HATPase_CckA-like

cd16919

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...

365-469

1.89e-12

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

Pssm-ID: 340396 [Multi-domain] Cd Length: 116 Bit Score: 64.32 E-value: 1.89e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 365 FKQVLSNLVSNAIK-FTERGQVTIRLQERSLDEGRAI----------VRVDVEDSGIGIAPADQARLFQPFIqVAKGrtV 433
Cdd:cd16919   1 LELAILNLAVNARDaMPEGGRLTIETSNQRVDADYALnyrdlipgnyVCLEVSDTGSGMPAEVLRRAFEPFF-TTKE--V 77

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598240 434 QGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:cd16919  78 GKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113

COG4192

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...

224-471

2.19e-12

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

Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 70.49 E-value: 2.19e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 224 ITERERLARQLREAmrQADEANRAK-SVFLATM---SHEIRTPMNAVIGILELVlqRLAPEQRERASLEVAYEAAGSLQL 299
Cdd:COG4192 407 IEERKRIEKNLRQT--QDELIQAAKmAVVGQTMtslAHELNQPLNAMSMYLFSA--KKALEQENYAQLPTSLDKIEGLIE 482

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 300 LIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEglARQKGLRLVVELDDAPgrDVLIDPLRFKQVLSNLVSNAIK- 378
Cdd:COG4192 483 RMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVE--SRAKPQQITLHIPDDL--MVQGDQVLLEQVLVNLLVNALDa 558

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 379 FTERGQVTIRLQERSLDegraiVRVDVEDSGIGIAPADqaRLFQPFIQvakgrTVQGGTGLGLAICRKLVDLMGGDVEMH 458
Cdd:COG4192 559 VATQPQISVDLLSNAEN-----LRVAISDNGNGWPLVD--KLFTPFTT-----TKEVGLGLGLSICRSIMQQFGGDLYLA 626

                       250
                ....*....|...
gi 15598240 459 SEPGKGTRVSLDL 471
Cdd:COG4192 627 STLERGAMVILEF 639

REC_TrrA-like

cd17554

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...

499-582

2.26e-12

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

Pssm-ID: 381106 [Multi-domain] Cd Length: 113 Bit Score: 64.16 E-value: 2.26e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqERcERRAPILIl 578
Cdd:cd17554   2 KILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EK-KPDLPVII- 77


                ....
gi 15598240 579 gYTA 582
Cdd:cd17554  78 -CTA 80

AmiR

COG3707

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...

496-620

4.51e-12

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: 65.36 E-value: 4.51e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 496 RRLHILIADDYPPNRVLLRQQLEFLGHRV-AEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIriqeRCERRAP 574
Cdd:COG3707   2 RGLRVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQI----SEERPAP 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15598240 575 ILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGR 620
Cdd:COG3707  78 VILL--TAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELALAR 121

marine_sort_HK

TIGR03785

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...

209-469

7.74e-12

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: 68.62 E-value: 7.74e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   209 DRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELvLQRLAPEQRERASLE 288
Cdd:TIGR03785 446 DSQGRISGAIPASRSRDEIGDLSRSFAQMVARLRQYTHYLENMSSRLSHELRTPVAVVRSSLEN-LELQALEQEKQKYLE 524

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   289 VAYEAAGSLQLLIGDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLarQKGLRLVVELDDAPgRDVLIDPLRFKQV 368
Cdd:TIGR03785 525 RAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVLSGCMQGYQMT--YPPQRFELNIPETP-LVMRGSPELIAQM 601

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   369 LSNLVSNAIKFT-ERGQVTIRLqerSLDEGRAIvrVDVEDSGIGIAPADQARLFQPFIQV-AKGRTVQGGTGLGLAICRK 446
Cdd:TIGR03785 602 LDKLVDNAREFSpEDGLIEVGL---SQNKSHAL--LTVSNEGPPLPEDMGEQLFDSMVSVrDQGAQDQPHLGLGLYIVRL 676

                         250       260
                  ....*....|....*....|....*.
gi 15598240   447 LVDLMGGDVE---MHSEPGKGTRVSL 469
Cdd:TIGR03785 677 IADFHQGRIQaenRQQNDGVVFRISL 702

HATPase_YcbM-like

cd16947

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

367-471

7.79e-12

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: 62.92 E-value: 7.79e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 367 QVLSNLVSNAIKFTERGqvtiRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGR-TVQGGTGLGLAICR 445
Cdd:cd16947  23 RILKNLISNAIKYGSDG----KFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRnSAKQGNGLGLTITK 98

                        90       100
                ....*....|....*....|....*.
gi 15598240 446 KLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16947  99 RLAESMGGSIYVNSKPYEKTVFTVTL 124

Hpt

pfam01627

Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...

655-731

8.85e-12

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

Pssm-ID: 426352 [Multi-domain] Cd Length: 84 Bit Score: 61.60 E-value: 8.85e-12

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240   655 SNRQDLQRLAILLREGDRTRLAEHAHRIKGAARMIGARTLLEACEALEDACrRSGDGECLQAPGERLRLALEALQEE 731
Cdd:pfam01627   9 EAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLL-REGELPLDPELLEALRDLLEALRAA 84

PRK11361

acetoacetate metabolism transcriptional regulator AtoC;

492-611

9.74e-12

acetoacetate metabolism transcriptional regulator AtoC;

Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 67.95 E-value: 9.74e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  492 MEPSRRlhILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercER 571
Cdd:PRK11361   1 MTAINR--ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSH---ET 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15598240  572 RAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:PRK11361  76 RTPVILM--TAYAEVETAVEALRCGAFDYVIKPFDLDELN 113

REC_RpfG-like

cd17551

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...

499-605

1.56e-11

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: 61.69 E-value: 1.56e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLG-HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCErRAPILI 577
Cdd:cd17551   2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLE-DVPIVM 80

                        90       100
                ....*....|....*....|....*...
gi 15598240 578 LgyTADAEPDEVQRCRDAGMDDCLFKPL 605
Cdd:cd17551  81 I--TADTDREVRLRALEAGATDFLTKPF 106

PRK10610

chemotaxis protein CheY;

496-618

1.58e-11

chemotaxis protein CheY;

Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 62.30 E-value: 1.58e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  496 RRLHILIADDYPPNRVLLRQQLEFLG-HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCERRAP 574
Cdd:PRK10610   4 KELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIR-ADGAMSALP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15598240  575 ILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSF 618
Cdd:PRK10610  83 VLMV--TAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIF 124

HATPase_NtrY-like

cd16944

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

361-471

2.05e-11

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: 61.40 E-value: 2.05e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFTE-----RGQVTIRLQErslDEGRAIVrVDVEDSGIGIAPADQARLFQPFIQvakgrTVQG 435
Cdd:cd16944   1 DTTQISQVLTNILKNAAEAIEgrpsdVGEVRIRVEA---DQDGRIV-LIVCDNGKGFPREMRHRATEPYVT-----TRPK 71

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15598240 436 GTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16944  72 GTGLGLAIVKKIMEEHGGRISLSNREAGGACIRIIL 107

REC

smart00448

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...

498-552

9.24e-11

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: 57.58 E-value: 9.24e-11

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 15598240    498 LHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMP 552
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55

HATPase_CpxA-like

cd16949

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

365-471

1.59e-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: 58.49 E-value: 1.59e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 365 FKQVLSNLVSNAIKFTeRGQVTIRLQErsldEGRAIVrVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAI 443
Cdd:cd16949   1 LARALENVLRNALRYS-PSKILLDISQ----DGDQWT-ITITDDGPGVPEDQLEQIFLPFYRVDSARDREsGGTGLGLAI 74

                        90       100
                ....*....|....*....|....*...
gi 15598240 444 CRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16949  75 AERAIEQHGGKIKASNRKPGGLRVRIWL 102

HATPase_BvrS-ChvG-like

cd16953

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

367-471

1.82e-10

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: 58.74 E-value: 1.82e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 367 QVLSNLVSNAIKFTERGQVTIRLqerSLDEGRAIVRVDVEDSGIGIAPADQARLFQPF-IQVAKGRTVQGGTGLGLAICR 445
Cdd:cd16953   3 QVLRNLIGNAISFSPPDTGRITV---SAMPTGKMVTISVEDEGPGIPQEKLESIFDRFyTERPANEAFGQHSGLGLSISR 79

                        90       100       110
                ....*....|....*....|....*....|
gi 15598240 446 KLVDLMGGDV--EMHSEPG--KGTRVSLDL 471
Cdd:cd16953  80 QIIEAHGGISvaENHNQPGqvIGARFTVQL 109

PAS

COG2202

PAS domain [Signal transduction mechanisms];

102-261

2.53e-10

PAS domain [Signal transduction mechanisms];

Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 61.58 E-value: 2.53e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQcLAVARG 181
Cdd:COG2202   1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLR-AALAGG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 182 GTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRT 261
Cdd:COG2202  80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159

REC_Rcp-like

cd17557

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...

499-610

3.46e-10

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: 58.20 E-value: 3.46e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALE-LWADERFE------VLISDCNMPRLNGYQLARRIRIQERC 569
Cdd:cd17557   1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDfLRGEGEYAdaprpdLILLDLNMPRMDGFEVLREIKADPDL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15598240 570 eRRAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:cd17557  81 -RRIPVVVL--TTSDAEEDIERAYELGANSYIVKPVDFEEF 118

REC_OmpR_CusR-like

cd19935

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...

500-604

7.15e-10

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

Pssm-ID: 381162 [Multi-domain] Cd Length: 100 Bit Score: 56.68 E-value: 7.15e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerrAPILILg 579
Cdd:cd19935   1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ---TPVLML- 76

                        90       100
                ....*....|....*....|....*.
gi 15598240 580 yTA-DAEPDEVqRCRDAGMDDCLFKP 604
Cdd:cd19935  77 -TArDSVEDRV-KGLDLGADDYLVKP 100

REC_OmpR_EcPhoP-like

cd19934

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...

500-610

9.29e-10

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381161 [Multi-domain] Cd Length: 117 Bit Score: 56.91 E-value: 9.29e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPILILg 579
Cdd:cd19934   1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE---GRATPVLIL- 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 580 yTA-DAEPDEVQRCrDAGMDDCLFKPLGLETL 610
Cdd:cd19934  77 -TArDSWQDKVEGL-DAGADDYLTKPFHIEEL 106

PRK11086

sensory histidine kinase DcuS; Provisional

339-471

1.20e-09

sensory histidine kinase DcuS; Provisional

Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 61.47 E-value: 1.20e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  339 ARQKGLRLVVELD----DAPGRD---VLIdplrfkQVLSNLVSN---AIKFTERGQVTIRLQERsldEGRAIVRVdvEDS 408
Cdd:PRK11086 407 ARELGITLIISEDsqlpDSGDEDqvhELI------TILGNLIENaleAVGGEEGGEISVSLHYR---NGWLHCEV--SDD 475

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598240  409 GIGIAPADQARLFQpfiqvaKGRTVQG-GTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:PRK11086 476 GPGIAPDEIDAIFD------KGYSTKGsNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFVQI 533

REC_YesN-like

cd17536

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...

500-564

1.24e-09

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: 56.58 E-value: 1.24e-09

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598240 500 ILIADDYPPNRVLLRQQL--EFLG-HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR 564
Cdd:cd17536   1 VLIVDDEPLIREGLKKLIdwEELGfEVVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIR 68

HPtr

COG2198

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];

222-737

1.24e-09

HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];

Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 61.99 E-value: 1.24e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 222 IDITERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEQRERASLEVAYEAAGSLQLLI 301
Cdd:COG2198 348 LLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLLLLLLLLL 427

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 302 GDILDVAKIESGHLTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFTE 381
Cdd:COG2198 428 LLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLV 507

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 382 RGQVTIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEP 461
Cdd:COG2198 508 AAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLLGGLLLLLLLLLLLLL 587

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 462 GKGTRVSLDLLLRQCGPKMPESGQDPLAASMEPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADER 541
Cdd:COG2198 588 LLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAAAAAALAA 667

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 542 FEVLISDCNMPRLNGYQLARRIRIQERCERRAPILILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGRD 621
Cdd:COG2198 668 LDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLLLLLLLAA 747

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 622 --------AAQPRGLYDAAALSSLGGDRPERLRELLETLLgSNRQDLQRLAILLREGDRTRLAEHAHRIKGAARMIGART 693
Cdd:COG2198 748 aaaaaaspAAPALPVLDLEALRRLGGDPELLRELLELFLE-ELPELLAELRQALAAGDLEALARLAHKLKGSAGNLGAPR 826

                       490       500       510       520
                ....*....|....*....|....*....|....*....|....
gi 15598240 694 LLEACEALEDACrRSGDGECLQAPGERLRLALEALQEELQEQLA 737
Cdd:COG2198 827 LAELAAELEQAA-RAGDLEEAEELLAELEAELERVLAALEALLA 869

REC_HupR-like

cd17569

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...

500-585

2.03e-09

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: 55.87 E-value: 2.03e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR-IQERCERrapILIL 578
Cdd:cd17569   3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVReRYPDTVR---ILLT 79


                ....*..
gi 15598240 579 GYtADAE 585
Cdd:cd17569  80 GY-ADLD 85

REC_OmpR_BsPhoP-like

cd19937

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...

501-604

2.25e-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: 55.74 E-value: 2.25e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 501 LIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcERRAPILILgy 580
Cdd:cd19937   1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPK-TSSIPIIML-- 77

                        90       100
                ....*....|....*....|....*
gi 15598240 581 TA-DAEPDEVQRCrDAGMDDCLFKP 604
Cdd:cd19937  78 TAkGEEFDKVLGL-ELGADDYITKP 101

HATPase_Phy-like

cd16932

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...

361-463

3.34e-09

Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana Phytochrome A, B, C, D and E; This family includes the histidine kinase-like ATPase (HATPase) domains of plant red/far-red photoreceptors, the phytochromes, and includes the Arabidopsis thaliana phytochrome family phyA-phyE. Following red light absorption, biologically inactive forms of phytochromes convert to active forms, which rapidly convert back to inactive forms upon far-red light irradiation. Phytochromes can be considered as having an N-terminal photosensory region to which a bilin chromophore is bound, and a C-terminal output region, which includes the HATPase domain represented here, and is involved in dimerization and presumably contributes to relaying the light signal to downstream signaling events.

Pssm-ID: 340409 [Multi-domain] Cd Length: 113 Bit Score: 54.97 E-value: 3.34e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFT--ERGQVTIRLQERSLDEGRAIVRVDVE----DSGIGIAPADQARLFQPfiqvAKGRTVQ 434
Cdd:cd16932   3 DQIRLQQVLADFLLNAVRFTpsPGGWVEIKVSPTKKQIGDGVHVIHLEfritHPGQGLPEELVQEMFEE----NQWTTQE 78

                        90       100
                ....*....|....*....|....*....
gi 15598240 435 GgtgLGLAICRKLVDLMGGDVEMHSEPGK 463
Cdd:cd16932  79 G---LGLSISRKLVKLMNGDVRYLREAGR 104

REC_RssB-like

cd17555

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...

500-605

3.66e-09

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

Pssm-ID: 381107 [Multi-domain] Cd Length: 116 Bit Score: 54.90 E-value: 3.66e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILIL- 578
Cdd:cd17555   3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQIT---KESPDTPVIVVs 79

                        90       100
                ....*....|....*....|....*....
gi 15598240 579 --GYTADAepdeVQRCRdAGMDDCLFKPL 605
Cdd:cd17555  80 gaGVMSDA----VEALR-LGAWDYLTKPI 103

REC_typeB_ARR-like

cd17584

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...

500-612

4.09e-09

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: 54.94 E-value: 4.09e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELW--ADERFEVLISDCNMPRLNGYQLARRIRIqercERRAPILI 577
Cdd:cd17584   1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRL----EMDLPVIM 76

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15598240 578 LgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRN 612
Cdd:cd17584  77 M--SADGSTSTVMKGLAHGACDYLLKPVSIEDLKN 109

REC_Ycf29

cd19927

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...

500-604

4.26e-09

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381154 [Multi-domain] Cd Length: 102 Bit Score: 54.31 E-value: 4.26e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeRRAPILILg 579
Cdd:cd19927   1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADF-DTIPVIFL- 78

                        90       100
                ....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd19927  79 -TAKGMTSDRIKGYNAGCDGYLSKP 102

REC_OmpR_ArcA_TorR-like

cd17619

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...

499-610

5.57e-09

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: 54.32 E-value: 5.57e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerrAPILIL 578
Cdd:cd17619   2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQSEV---GIILVT 78

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598240 579 GytadaEPDEVQRC--RDAGMDDCLFKPLGLETL 610
Cdd:cd17619  79 G-----RDDEVDRIvgLEIGADDYVTKPFNPREL 107

YesM

COG2972

Sensor histidine kinase YesM [Signal transduction mechanisms];

320-471

7.28e-09

Sensor histidine kinase YesM [Signal transduction mechanisms];

Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 58.88 E-value: 7.28e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 320 ERVRLRHVVESVRRMFEGL-AR-QKGLRLVVELDDAPgRDVLIDPLrfkqVLSNLVSNAIKF-----TERGQVTIRLQEr 392
Cdd:COG2972 295 ELVTLEEELELIKSYLEIQkLRfGDRLEVEIEIDEEL-LDLLIPKL----ILQPLVENAIEHgiepkEGGGTIRISIRK- 368

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 393 slDEGRAIVRVdvEDSGIGIAPADQARLFQPFiqvakgRTVQGGTGLGLAICRKLVDLMGGD---VEMHSEPGKGTRVSL 469
Cdd:COG2972 369 --EGDRLVITV--EDNGVGMPEEKLEKLLEEL------SSKGEGRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTI 438


                ..
gi 15598240 470 DL 471
Cdd:COG2972 439 RI 440

RsbW

COG2172

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

328-469

8.07e-09

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

Pssm-ID: 441775 [Multi-domain] Cd Length: 127 Bit Score: 54.53 E-value: 8.07e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 328 VESVRRMFEGLARQKGLRlvvelddapgrDVLIDplRFKQVLSNLVSNAIK----FTERGQVTIRLqerSLDEGRaiVRV 403
Cdd:COG2172  11 LGLARRAVRALLRELGLD-----------EDDAD--DLVLAVSEAVTNAVRhaygGDPDGPVEVEL---ELDPDG--LEI 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15598240 404 DVEDSGIGIAPADqarlfqpfiqVAKGRTVQGGTGLGLAICRKLVDlmggDVEMHSEPGkGTRVSL 469
Cdd:COG2172  73 EVRDEGPGFDPED----------LPDPYSTLAEGGRGLFLIRRLMD----EVEYESDPG-GTTVRL 123

HPT

cd00088

Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...

658-733

1.36e-08

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

Pssm-ID: 238041 [Multi-domain] Cd Length: 94 Bit Score: 52.77 E-value: 1.36e-08

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15598240 658 QDLQR-LAILLREGDRTRLAEHAHRIKGAARMIGARTLLEACEALEDACRRSGDGECLQAPGERLRL-ALEALQEELQ 733
Cdd:cd00088  17 EELERaLLELEDAEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLDALRDGLEVTPELIDLLLdALDALKAELE 94

REC_OmpR_DrrD-like

cd17625

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...

501-611

1.72e-08

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: 52.99 E-value: 1.72e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 501 LIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCErrAPILILgy 580
Cdd:cd17625   1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLR-EEGIE--TPVLLL-- 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 581 TA-DAEPDEVqRCRDAGMDDCLFKPLGLETLR 611
Cdd:cd17625  76 TAlDAVEDRV-KGLDLGADDYLPKPFSLAELL 106

cpxA

PRK09470

envelope stress sensor histidine kinase CpxA;

252-443

2.27e-08

envelope stress sensor histidine kinase CpxA;

Pssm-ID: 236532 [Multi-domain] Cd Length: 461 Bit Score: 57.25 E-value: 2.27e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  252 LATMSHEIRTPMNAvigiLELVLQRLAPEQRERASLEVAYEAAGSLQLLIGDILDVAKIESgHLTLTPERVRLRH----V 327
Cdd:PRK09470 247 LSDISHELRTPLTR----LQLATALLRRRQGESKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSlwseV 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  328 VESVRrmFEglARQKGLRLVVELDdaPGRDVLI-DPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSLdegraivRVDV 405
Cdd:PRK09470 322 LEDAK--FE--AEQMGKSLTVSAP--PGPWPINgNPNALASALENIVRNALRYShTKIEVAFSVDKDGL-------TITV 388

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 15598240  406 EDSGIGIAPADQARLFQPFIQVAKGRTVQ-GGTGLGLAI 443
Cdd:PRK09470 389 DDDGPGVPEEEREQIFRPFYRVDEARDREsGGTGLGLAI 427

HATPase_PhoQ-like

cd16954

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

328-468

2.80e-08

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: 53.02 E-value: 2.80e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 328 VESVRRMFEGLARQKGLRLVVELDdaPGRDVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSLdegraivRVDVE 406
Cdd:cd16954   3 LDSLCSALNKVYQRKGVSISLDIS--PELRFPGERNDLMELLGNLLDNACKWClEFVEVTARQTDGGL-------HLIVD 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15598240 407 DSGIGIAPADQARLFQPFIQVAKGRTvqgGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVS 468
Cdd:cd16954  74 DDGPGVPESQRSKIFQRGQRLDEQRP---GQGLGLAIAKEIVEQYGGELSLSDSPLGGARFE 132

LytT

COG3279

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...

498-585

3.47e-08

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

Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 54.82 E-value: 3.47e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPPNRVLLRQQLE-FLGHR-VAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqercERRAPI 575
Cdd:COG3279   2 MKILIVDDEPLARERLERLLEkYPDLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR-----ELDPPP 76

                        90
                ....*....|
gi 15598240 576 LILGYTADAE 585
Cdd:COG3279  77 PIIFTTAYDE 86

HATPase_VanS-like

cd16923

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

368-460

3.75e-08

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: 51.62 E-value: 3.75e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIKFTERgQVTIRLQERSLDEgraIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVqGGTGLGLAICRKL 447
Cdd:cd16923   4 VFSNLLSNAIKYSPE-NTRIYITSFLTDD---VVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNT-EGAGLGLSIAKAI 78

                        90
                ....*....|...
gi 15598240 448 VDLMGGDVEMHSE 460
Cdd:cd16923  79 IELHGGSASAEYD 91

ComP

COG4585

Signal transduction histidine kinase ComP [Signal transduction mechanisms];

226-471

4.07e-08

Signal transduction histidine kinase ComP [Signal transduction mechanisms];

Pssm-ID: 443642 [Multi-domain] Cd Length: 252 Bit Score: 55.01 E-value: 4.07e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 226 ERERLARQLREAMRQADEANRAKsvfLA-----TMSHEIrtpmnAVIGILELVLQRLAPEQRERASLEVAyEAAGSLQLL 300
Cdd:COG4585  34 RAAELERELAARAEEAREEERRR---IArelhdGVGQSL-----SAIKLQLEAARRLLDADPEAAREELE-EIRELAREA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 301 IGDILDVAKiesghlTLTPERVRLRHVVESVRRMFEGLARQKGLRLVVELDDAPGR---DVLIDPLRfkqVLSNLVSNAI 377
Cdd:COG4585 105 LAELRRLVR------GLRPPALDDLGLAAALEELAERLLRAAGIRVELDVDGDPDRlppEVELALYR---IVQEALTNAL 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 378 KFTERGQVTIRLqerSLDEGRaiVRVDVEDSGIGIAPADQArlfqpfiqvakgrtvqgGTGLGLAICRKLVDLMGGDVEM 457
Cdd:COG4585 176 KHAGATRVTVTL---EVDDGE--LTLTVRDDGVGFDPEAAP-----------------GGGLGLRGMRERAEALGGTLTI 233

                       250
                ....*....|....
gi 15598240 458 HSEPGKGTRVSLDL 471
Cdd:COG4585 234 GSAPGGGTRVRATL 247

REC_hyHK_blue-like

cd18161

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...

500-604

5.80e-08

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: 51.19 E-value: 5.80e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALE-LWADERFEVLISDCNMPR-LNGYQLARRIRIqerceRRAPILI 577
Cdd:cd18161   1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDlLESGPDIDLLVTDVIMPGgMNGSQLAEEARR-----RRPDLKV 75

                        90       100
                ....*....|....*....|....*..
gi 15598240 578 LGYTADAEPDEVQRCRDAGMdDCLFKP 604
Cdd:cd18161  76 LLTSGYAENAIEGGDLAPGV-DVLSKP 101

HATPase_DpiB-CitA-like

cd16915

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

368-469

6.23e-08

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: 51.13 E-value: 6.23e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIKFTER-----GQVTIRLQerslDEGRAIVrVDVEDSGIGIAPADQARLFQpfiqvaKGRTVQGGT--GLG 440
Cdd:cd16915   4 IVGNLIDNALDALAAtgapnKQVEVFLR----DEGDDLV-IEVRDTGPGIAPELRDKVFE------RGVSTKGQGerGIG 72

                        90       100
                ....*....|....*....|....*....
gi 15598240 441 LAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:cd16915  73 LALVRQSVERLGGSITVESEPGGGTTFSI 101

HATPase_RsbT-like

cd16934

Histidine kinase-like ATPase domain of the anti sigma-B factor Bacillus subtilis serine ...

331-467

8.60e-08

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: 51.22 E-value: 8.60e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 331 VRRMFEGLARQKGLRLVvelddapgrdvliDPLRFKQVLSNLVSNAIKFTERGQVTIRLQersLDEGRAIVRVDVEDSGI 410
Cdd:cd16934   5 ARRAARELARRLGLSEV-------------RQAEIATAVTELARNLLKHAGGGQVLLEVV---AEGGRVALEILAVDQGP 68

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240 411 GIAPADQARLfqpfiqvaKGRTVQGGTGLGLAICRKLVDlmggDVEMHSEPGKGTRV 467
Cdd:cd16934  69 GIADVDEALR--------DGFSTGGGLGLGLGGVRRLAD----EFDLHSAPGRGTVV 113

HATPase_SpoIIAB-like

cd16942

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...

336-469

9.18e-08

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.

Pssm-ID: 340418 [Multi-domain] Cd Length: 135 Bit Score: 51.77 E-value: 9.18e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 336 EGLARQKGLRLVVELDdaPGRDVLIDplrFKQVLSNLVSNAI----KFTERGQVTIrlqERSLDEGraIVRVDVEDSGIG 411
Cdd:cd16942  15 ESFARVTVAAFVAQLD--PTIDELTE---IKTVVSEAVTNAIihgyNNDPNGIVSI---SVIIEDG--VVHLTVRDEGVG 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598240 412 IAPADQARlfQPFIQVakgRTVQGGTGLGLAICRKLVDlmggDVEMHSEPGKGTRVSL 469
Cdd:cd16942  85 IPDIEEAR--QPLFTT---KPELERSGMGFTIMENFMD----EVIVESEVNKGTTVYL 133

REC_CheB-like

cd17541

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...

500-607

9.30e-08

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: 51.24 E-value: 9.30e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHR--VAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIqercERRAPILI 577
Cdd:cd17541   3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMA----ERPTPVVM 78

                        90       100       110
                ....*....|....*....|....*....|
gi 15598240 578 LGYTADAEPDEVQRCRDAGMDDCLFKPLGL 607
Cdd:cd17541  79 VSSLTEEGAEITLEALELGAVDFIAKPSGG 108

PRK10337

sensor protein QseC; Provisional

251-469

1.14e-07

sensor protein QseC; Provisional

Pssm-ID: 182388 [Multi-domain] Cd Length: 449 Bit Score: 55.04 E-value: 1.14e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  251 FLATMSHEIRTPMNAVIGILELV-LQRLAPEQRERA--SLEVAYEAAGSL--QLLIgdildVAKIESGHLTLTPERVRLR 325
Cdd:PRK10337 240 FTSDAAHELRSPLAALKVQTEVAqLSDDDPQARKKAllQLHAGIDRATRLvdQLLT-----LSRLDSLDNLQDVAEIPLE 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  326 HVVESVRRMFEGLARQKG--LRLvveldDAPGRDVL--IDPLRFKQVLSNLVSNAIKFTERG-QVTIRLQERSLDegrai 400
Cdd:PRK10337 315 DLLQSAVMDIYHTAQQAGidVRL-----TLNAHPVIrtGQPLLLSLLVRNLLDNAIRYSPQGsVVDVTLNARNFT----- 384

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598240  401 vrvdVEDSGIGIAPADQARLFQPFIQvAKGRTvQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:PRK10337 385 ----VRDNGPGVTPEALARIGERFYR-PPGQE-ATGSGLGLSIVRRIAKLHGMNVSFGNAPEGGFEAKV 447

REC_LytTR_AlgR-like

cd17532

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...

500-582

1.37e-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: 50.61 E-value: 1.37e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHR--VAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIriqerCERRAPILI 577
Cdd:cd17532   1 ALIVDDEPLAREELRYLLEEHPDIeiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKL-----SKLAKPPLI 75


                ....*
gi 15598240 578 LGYTA 582
Cdd:cd17532  76 VFVTA 80

ompR

PRK09468

osmolarity response regulator; Provisional

493-604

2.01e-07

osmolarity response regulator; Provisional

Pssm-ID: 181883 [Multi-domain] Cd Length: 239 Bit Score: 52.67 E-value: 2.01e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  493 EPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERR 572
Cdd:PRK09468   1 MMQENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQ---NNP 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598240  573 APILILgytaDAEPDEVQRCR--DAGMDDCLFKP 604
Cdd:PRK09468  78 TPIIML----TAKGEEVDRIVglEIGADDYLPKP 107

COG3920

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...

92-475

2.03e-07

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

Pssm-ID: 443125 [Multi-domain] Cd Length: 495 Bit Score: 54.14 E-value: 2.03e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  92 VLQLRLRRWQRTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLM 171
Cdd:COG3920 144 LALAELAVALAELAAALLLLAEELAALRLAAAALLLLLAALLDLGLALAALAAAALLALLLALELLLALLLLLLLLLALL 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 172 HQQCLAVARGGTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDITERERlarqlREAMRQADEANRAKSVF 251
Cdd:COG3920 224 LVLLAALLRLRAAVLEELERRRRARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITER-----KRAEEELEASLEEKELL 298

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 252 LATMSHEIRTPMNAVIGILELvlqrlapeQRERASLEVAYEAAGSLQlliGDILDVAKIesgHLTLTP----ERVRLRHV 327
Cdd:COG3920 299 LRELHHRVKNNLQVVSSLLRL--------QARRADDPEAREALEESQ---NRIQALALV---HELLYQsedwEGVDLRDY 364

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 328 VESVRRMFEGLARQKGLRLVVELDDAP-GRDVLIdPLRFkqVLSNLVSNAIKF----TERGQVTIRLqerSLDEGRaiVR 402
Cdd:COG3920 365 LRELLEPLRDSYGGRGIRIELDGPDVElPADAAV-PLGL--ILNELVTNALKHaflsGEGGRIRVSW---RREDGR--LR 436

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15598240 403 VDVEDSGIGIAPadqarlfqpfiqvakGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPgkGTRVSLDLLLRQ 475
Cdd:COG3920 437 LTVSDNGVGLPE---------------DVDPPARKGLGLRLIRALVRQLGGTLELDRPE--GTRVRITFPLAE 492

CitB

COG2197

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...

497-563

3.02e-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: 49.89 E-value: 3.02e-07

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15598240 497 RLHILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRI 563
Cdd:COG2197   1 MIRVLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69

PAS_4

pfam08448

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...

118-229

3.51e-07

Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 49.33 E-value: 3.51e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   118 VDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSdWVEGSKARLMHQQCLAVARGGTASFTDMAVRIGgql 197
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLERALRRALEGEEPIDFLEELLLNG--- 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 15598240   198 lEIHHW---VTPYRDRQGRVLGLMNGWIDITERER 229
Cdd:pfam08448  77 -EERHYelrLTPLRDPDGEVIGVLVISRDITERRR 110

COG4567

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...

499-625

3.65e-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: 50.69 E-value: 3.65e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqERCERRAPILIL 578
Cdd:COG4567   6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALR--ERDPDARIVVLT 83

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15598240 579 GYTADAepDEVQRCRdAGMDDCLFKPLGLETLRNYLATSFGRDAAQP 625
Cdd:COG4567  84 GYASIA--TAVEAIK-LGADDYLAKPADADDLLAALERAEGDAPAPP 127

REC_OmpR_PmrA-like

cd17624

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...

500-610

5.15e-07

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: 49.02 E-value: 5.15e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDyppNRVL---LRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERcerRAPIL 576
Cdd:cd17624   1 ILLVED---DALLgdgLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQ---SLPVL 74

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598240 577 ILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:cd17624  75 IL--TARDGVDDRVAGLDAGADDYLVKPFALEEL 106

PRK10755

two-component system sensor histidine kinase PmrB;

223-471

5.20e-07

two-component system sensor histidine kinase PmrB;

Pssm-ID: 236751 [Multi-domain] Cd Length: 356 Bit Score: 52.28 E-value: 5.20e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  223 DITERERLARQLREAMRQADEANRAKSVFLATMSHEIRTPMNAVIGILELVLQRLAPEqrerASLEVAyeAAGSLQLLIG 302
Cdd:PRK10755 112 STLEIEAVTSALNQLVSRLTSTLDQERLFTADVAHELRTPLAGIRLHLELLEKQHHID----VAPLIA--RLDQMMHTVE 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  303 DILDVAKIE----SGHLtltpERVRLRH-VVESVRRMFEGLARQKGLRLVVELDDAPGRdVLIDPLRFKQVLSNLVSNAI 377
Cdd:PRK10755 186 QLLQLARAGqsfsSGHY----QTVKLLEdVILPSQDELSEMLEQRQQTLLLPESAADIT-VQGDATLLRLLLRNLVENAH 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  378 KFT-ERGQVTIRLQErslDEGRAIVRvdVEDSGIGIAPADQARLFQPFIqvakgRTVQ--GGTGLGLAICRKLVDLMGGD 454
Cdd:PRK10755 261 RYSpEGSTITIKLSQ---EDGGAVLA--VEDEGPGIDESKCGELSKAFV-----RMDSryGGIGLGLSIVSRITQLHHGQ 330

                        250
                 ....*....|....*....
gi 15598240  455 --VEMHSEPGkGTRVSLDL 471
Cdd:PRK10755 331 ffLQNRQERS-GTRAWVWL 348

orf27

CHL00148

Ycf27; Reviewed

492-604

5.87e-07

Ycf27; Reviewed

Pssm-ID: 214376 [Multi-domain] Cd Length: 240 Bit Score: 51.26 E-value: 5.87e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  492 MEPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIriqeRCER 571
Cdd:CHL00148   1 TMENSKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEI----RKES 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598240  572 RAPILILGYTADAEpDEVQRCRdAGMDDCLFKP 604
Cdd:CHL00148  77 DVPIIMLTALGDVS-DRITGLE-LGADDYVVKP 107

REC_OmpR_MtPhoP-like

cd17615

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...

500-610

1.16e-06

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: 48.12 E-value: 1.16e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILILg 579
Cdd:cd17615   2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLR---ADGPDVPVLFL- 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 580 yTA-DAEPDEVQRCrDAGMDDCLFKPLGLETL 610
Cdd:cd17615  78 -TAkDSVEDRIAGL-TAGGDDYVTKPFSLEEV 107

HATPase_UhpB-NarQ-NarX-like

cd16917

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

373-469

1.38e-06

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

Pssm-ID: 340394 [Multi-domain] Cd Length: 87 Bit Score: 46.78 E-value: 1.38e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 373 VSNAIKFTERGQVTIRLQErslDEGRaiVRVDVEDSGIGIAPADQArlfqpfiqvakgrtvqGGTGLGLAICRKLVDLMG 452
Cdd:cd16917   9 LTNALKHAGASRVRVTLSY---TADE--LTLTVVDDGVGFDGPAPP----------------GGGGFGLLGMRERAELLG 67

                        90
                ....*....|....*..
gi 15598240 453 GDVEMHSEPGKGTRVSL 469
Cdd:cd16917  68 GTLTIGSRPGGGTRVTA 84

REC_CpdR_CckA-like

cd18160

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...

500-584

1.61e-06

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: 47.11 E-value: 1.61e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALE-LWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPIL-I 577
Cdd:cd18160   2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEkLQQGKDIDIVVTDIVMPEMDGIELAREAR---KIDPDVKILfI 78


                ....*..
gi 15598240 578 LGYTADA 584
Cdd:cd18160  79 SGGAAAA 85

REC_Spo0F-like

cd17553

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...

500-611

1.68e-06

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: 47.55 E-value: 1.68e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerrAPILILG 579
Cdd:cd17553   3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVID-----ENIRVII 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 580 YTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:cd17553  78 MTAYGELDMIQESKELGALTHFAKPFDIDEIR 109

REC_OmpR_YycF-like

cd17614

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...

500-610

2.50e-06

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: 47.03 E-value: 2.50e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQerceRRAPILILg 579
Cdd:cd17614   1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT----SNVPIIML- 75

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 580 yTA-DAEPDEVQRCrDAGMDDCLFKPLGLETL 610
Cdd:cd17614  76 -TAkDSEVDKVLGL-ELGADDYVTKPFSNREL 105

PRK10693

two-component system response regulator RssB;

525-605

3.99e-06

two-component system response regulator RssB;

Pssm-ID: 182652 [Multi-domain] Cd Length: 303 Bit Score: 49.22 E-value: 3.99e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  525 AEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPILILGYTAD-AEPDEVQRCrdaGMDDCLFK 603
Cdd:PRK10693   1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNR---GDQTPVLVISATENmADIAKALRL---GVQDVLLK 74


                 ..
gi 15598240  604 PL 605
Cdd:PRK10693  75 PV 76

PRK15479

transcriptional regulator TctD;

498-628

4.26e-06

transcriptional regulator TctD;

Pssm-ID: 185376 [Multi-domain] Cd Length: 221 Bit Score: 48.56 E-value: 4.26e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  498 LHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILI 577
Cdd:PRK15479   1 MRLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLR---KRGQTLPVLL 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15598240  578 LgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSFGRDAAQPRGL 628
Cdd:PRK15479  78 L--TARSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSAGQVQEV 126

PLN03029

type-a response regulator protein; Provisional

491-610

5.81e-06

type-a response regulator protein; Provisional

Pssm-ID: 215544 [Multi-domain] Cd Length: 222 Bit Score: 48.11 E-value: 5.81e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  491 SMEPSRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALE---LWADER---------------FEV--LISDCN 550
Cdd:PLN03029   2 GITTESQFHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKflgLHEDDRsnpdtpsvspnshqeVEVnlIITDYC 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  551 MPRLNGYQLARRIRiQERCERRAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:PLN03029  82 MPGMTGYDLLKKIK-ESSSLRNIPVVIM--SSENVPSRITRCLEEGAEEFFLKPVQLSDL 138

REC_NtrX-like

cd17550

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...

500-564

1.00e-05

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: 45.18 E-value: 1.00e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR 564
Cdd:cd17550   1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIK 65

HATPase_SpaK_NisK-like

cd16975

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

361-469

1.03e-05

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: 44.76 E-value: 1.03e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFT-ERGQVTIrlqerSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGL 439
Cdd:cd16975   1 DTLLLSRALINIISNACQYApEGGTVSI-----SIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGHYGM 75

                        90       100       110
                ....*....|....*....|....*....|
gi 15598240 440 GLAICRKLVDLMGGDVEMHSEPGKGTRVSL 469
Cdd:cd16975  76 GLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105

REC_CheY

cd17542

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...

500-605

1.09e-05

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: 44.96 E-value: 1.09e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLG-HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqeRCERRAPILIL 578
Cdd:cd17542   3 VLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIK---KIDPNAKVIMC 79

                        90       100
                ....*....|....*....|....*..
gi 15598240 579 gyTADAEPDEVQRCRDAGMDDCLFKPL 605
Cdd:cd17542  80 --SAMGQEEMVKEAIKAGAKDFIVKPF 104

REC_typeA_ARR

cd17581

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...

500-607

1.14e-05

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

Pssm-ID: 381119 [Multi-domain] Cd Length: 122 Bit Score: 45.05 E-value: 1.14e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFE-----------VLISDCNMPRLNGYQLARRIRIQER 568
Cdd:cd17581   1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEdssnfnepkvnMIITDYCMPGMTGYDLLKKVKESSA 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598240 569 CeRRAPILILgyTADAEPDEVQRCRDAGMDDCLFKPLGL 607
Cdd:cd17581  81 L-KEIPVVIM--SSENIPTRISRCLEEGAEDFLLKPVKL 116

REC_DC-like

cd17534

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...

500-611

1.38e-05

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: 44.71 E-value: 1.38e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAE-AEDGQVALELWADERFEVLISDCNMP-RLNGYQLARRIRiqERCerRAPILI 577
Cdd:cd17534   3 ILIVEDEAIIALDLKEILESLGYEVVGiADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIR--EKF--DIPVIF 78

                        90       100       110
                ....*....|....*....|....*....|....
gi 15598240 578 LgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLR 611
Cdd:cd17534  79 L--TAYSDEETLERAKETNPYGYLVKPFNERELK 110

PRK15115

response regulator GlrR; Provisional

499-610

1.81e-05

response regulator GlrR; Provisional

Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 47.91 E-value: 1.81e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIriqERCERRAPILIL 578
Cdd:PRK15115   7 HLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEI---QKVQPGMPVIIL 83

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598240  579 gyTADAE-PDEVQRCRDaGMDDCLFKPLGLETL 610
Cdd:PRK15115  84 --TAHGSiPDAVAATQQ-GVFSFLTKPVDRDAL 113

REC_DctD-like

cd17549

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...

500-564

2.96e-05

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: 44.02 E-value: 2.96e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR 564
Cdd:cd17549   1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIR 65

PRK10529

DNA-binding transcriptional activator KdpE; Provisional

500-626

3.81e-05

DNA-binding transcriptional activator KdpE; Provisional

Pssm-ID: 182522 [Multi-domain] Cd Length: 225 Bit Score: 45.57 E-value: 3.81e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerRAPILILG 579
Cdd:PRK10529   4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWS----AIPVIVLS 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 15598240  580 yTADAEPDEVQrCRDAGMDDCLFKPLGLETLRNYLATSFGRDAAQPR 626
Cdd:PRK10529  80 -ARSEESDKIA-ALDAGADDYLSKPFGIGELQARLRVALRRHSATPA 124

REC_TPR

cd17589

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...

500-564

5.12e-05

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: 43.02 E-value: 5.12e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLG-HRVAEAEDGQVALELWADERFEVLISDCNM-PRLNGYQLARRIR 564
Cdd:cd17589   1 FLIVDDQPTFRSMLKSMLRSLGvTRIDTASSGEEALRMCENKTYDIVLCDYNLgKGKNGQQLLEELR 67

HATPase_ETR2_ERS2-EIN4-like

cd16938

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...

361-471

6.50e-05

Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related domains; This family includes the histidine kinase-like ATPase domains (HATPase) of three out of the five receptors that recognize the plant hormone ethylene in Arabidopsis thaliana. These three proteins have been classified as belonging to subfamily 2: ETR2, ERS2, and EIN4. They lack most of the motifs characteristic of histidine kinases, and EIN4 is the only one in this group containing the conserved histidine that is phosphorylated in two-component and phosphorelay systems. This family also includes the HATPase domains of Escherichia coli RcsD phosphotransferase which is a component of the Rcs-signaling system, a complex multistep phosphorelay involving five proteins, and is involved in many transcriptional networks such as cell division, biofilm formation, and virulence, among others. Also included is Schizosaccharomyces pombe Mak3 (Phk1) which participates in a multi-step two-component related system which regulates H2O2-induced activation of the Sty1 stress-activated protein kinase pathway. Most proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a GAF sensor domain; most are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.

Pssm-ID: 340415 [Multi-domain] Cd Length: 133 Bit Score: 43.22 E-value: 6.50e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 361 DPLRFKQVLSNLVSNAIKFTER-GQVTIRL------QERS-LDEGRAIVRVDVEDSGI----GIAPADQARLFQPFIQVA 428
Cdd:cd16938   8 DERRVFQVLLHMLGNLLKMRNGgGNITFRVfleggsEDRSdRDWGPWRPSMSDESVEIrfevEINDSGSPSIESASMRNS 87

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15598240 429 KGRTVQG---GTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16938  88 LNRRYNLselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133

REC_OmpR_NsrR-like

cd18159

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...

500-610

6.73e-05

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381143 [Multi-domain] Cd Length: 113 Bit Score: 42.65 E-value: 6.73e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerRAPILILG 579
Cdd:cd18159   1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQIS----NVPIIFIS 76

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 580 yTADAEPDEVqRCRDAGMDDCLFKPLGLETL 610
Cdd:cd18159  77 -SRDDNMDQV-MAINMGGDDYITKPFDLDVL 105

pleD

PRK09581

response regulator PleD; Reviewed

500-604

7.93e-05

response regulator PleD; Reviewed

Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 45.66 E-value: 7.93e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCeRRAPILILg 579
Cdd:PRK09581   5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPAT-THIPVVMV- 82

                         90       100
                 ....*....|....*....|....*
gi 15598240  580 yTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:PRK09581  83 -TALDDPEDRVRGLEAGADDFLTKP 106

PRK10766

two-component system response regulator TorR;

499-610

7.96e-05

two-component system response regulator TorR;

Pssm-ID: 182711 [Multi-domain] Cd Length: 221 Bit Score: 44.64 E-value: 7.96e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerrAPILIL 578
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRSTV---GIILVT 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15598240  579 GYTadaepDEVQRC--RDAGMDDCLFKPLGLETL 610
Cdd:PRK10766  81 GRT-----DSIDRIvgLEMGADDYVTKPLELREL 109

REC_OmpR_CpxR

cd17623

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...

500-604

8.07e-05

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: 42.68 E-value: 8.07e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerraPILILg 579
Cdd:cd17623   1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQV----PVLML- 75

                        90       100
                ....*....|....*....|....*..
gi 15598240 580 ytaDAEPDEVQRC--RDAGMDDCLFKP 604
Cdd:cd17623  76 ---TARGDDIDRIlgLELGADDYLPKP 99

HATPase_YpdA-YehU-LytS-like

cd16924

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

368-471

8.22e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; 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. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.

Pssm-ID: 340401 [Multi-domain] Cd Length: 103 Bit Score: 42.43 E-value: 8.22e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIKFTergqvtirlQERSLDEGRAIVRVDVEDSGIGIAPADQARLFQPFIQVAKGRTVQGGTGLGLAICRKL 447
Cdd:cd16924   5 TLQPLVENAIQHG---------LSPLTDKGVVTISALKEDNHVMIEVEDNGRGIDPKVLNILGKKPKEGNGIGLYNVHQR 75

                        90       100
                ....*....|....*....|....*..
gi 15598240 448 VDLMGGD---VEMHSEPGKGTRVSLDL 471
Cdd:cd16924  76 LILLFGEdygIHIASEPDKGTRITFTI 102

REC_citrate_TCS

cd19925

phosphoacceptor receiver (REC) domain of citrate family two-component system response ...

498-615

8.71e-05

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: 42.62 E-value: 8.71e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 498 LHILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqercERRAPI 575
Cdd:cd19925   1 INVLIVEDDPMVAEIHRAYVEQVPgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELR-----AAGHDV 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15598240 576 LILGYTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLA 615
Cdd:cd19925  76 DVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLE 115

HPT

smart00073

Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...

655-712

8.88e-05

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

Pssm-ID: 197502 [Multi-domain] Cd Length: 92 Bit Score: 41.85 E-value: 8.88e-05

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 15598240    655 SNRQDLQRLAILLREGDRTRLAEHAHRIKGAARMIGARTLLEACEALEDACRRSGDGE 712
Cdd:smart00073  16 SLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLDALRSGE 73

HATPase_RsbW-like

cd16936

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase ...

368-471

1.01e-04

Histidine kinase-like ATPase domain of RsbW, an anti sigma-B factor and serine-protein kinase involved in regulating sigma-B during stress in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of RsbW, an anti sigma-B factor as well as a serine-protein kinase involved in regulating sigma-B during stress in Bacilli. The alternative sigma factor sigma-B is an important regulator of the general stress response of Bacillus cereus and B. subtilis. RsbW is an anti-sigma factor while RsbV is an anti-sigma factor antagonist (anti-anti-sigma factor). RsbW can also act as a kinase on RsbV. In a partner-switching mechanism, RsbW, RsbV, and sigma-B participate as follows: in non-stressed cells, sigma-B is present in an inactive form complexed with RsbW; in this form, sigma-B is unable to bind to RNA polymerase. Under stress, RsbV binds to RsbW, forming an RsbV-RsbW complex, and sigma-B is released to bind to RNA polymerase. RsbW may then act as a kinase on RsbV, phosphorylating a serine residue; RsbW is then released to bind to sigma-B, hence blocking its ability to bind RNA polymerase. A phosphatase then dephosphorylates RsbV so that it can again form a complex with RsbW, leading to the release of sigma-B.

Pssm-ID: 340413 [Multi-domain] Cd Length: 91 Bit Score: 41.48 E-value: 1.01e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIK--FTERGQVTIRLqERSLDEGRaiVRVDVEDSGigiAPADQARLFQPfiqvakGRTVQGGtGLGLAICR 445
Cdd:cd16936   4 AVSEAVTNAVRhaYRHDGPGPVRL-ELDLDPDR--LRVEVTDSG---PGFDPLRPADP------DAGLREG-GRGLALIR 70

                        90       100
                ....*....|....*....|....*.
gi 15598240 446 KLVDlmggDVEMHSEPGkGTRVSLDL 471
Cdd:cd16936  71 ALMD----EVGYRRTPG-GKTVWLEL 91

REC_HupR

cd17596

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...

500-612

1.12e-04

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: 42.74 E-value: 1.12e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLE--FlghRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqERCERRAPILI 577
Cdd:cd17596   3 ILVVDDEVRSLEALRRTLEedF---DVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVR--ERWPEVVRIII 77

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15598240 578 LGYTaDAEpDEVQRCRDAGMDDCLFKPLG----LETLRN 612
Cdd:cd17596  78 SGYT-DSE-DIIAGINEAGIYQYLTKPWHpdqlLLTVRN 114

PRK11173

two-component response regulator; Provisional

499-604

1.21e-04

two-component response regulator; Provisional

Pssm-ID: 183013 [Multi-domain] Cd Length: 237 Bit Score: 44.24 E-value: 1.21e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqercERRAPILIL 578
Cdd:PRK11173   5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELR-----EQANVALMF 79

                         90       100
                 ....*....|....*....|....*.
gi 15598240  579 GYTADAEPDEVQRCrDAGMDDCLFKP 604
Cdd:PRK11173  80 LTGRDNEVDKILGL-EIGADDYITKP 104

PRK09958

acid-sensing system DNA-binding response regulator EvgA;

501-624

1.27e-04

acid-sensing system DNA-binding response regulator EvgA;

Pssm-ID: 182168 [Multi-domain] Cd Length: 204 Bit Score: 43.73 E-value: 1.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  501 LIADDYPPNRVLLRQQLEFLGHRV-AEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiqercERRAPILILG 579
Cdd:PRK09958   4 IIIDDHPLAIAAIRNLLIKNDIEIlAELTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLR-----KRQYSGIIII 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15598240  580 YTADAEPDEVQRCRDAGMDDCLFKPLGLEtlrNYLATSfgrDAAQ 624
Cdd:PRK09958  79 VSAKNDHFYGKHCADAGANGFVSKKEGMN---NIIAAI---EAAK 117

PRK10815

two-component system sensor histidine kinase PhoQ;

252-467

1.49e-04

two-component system sensor histidine kinase PhoQ;

Pssm-ID: 182754 [Multi-domain] Cd Length: 485 Bit Score: 45.01 E-value: 1.49e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  252 LATMSHEIRTPMnAVigiLELVLQRLAPEQR---ERASlEVAYEAAGSLQLLIGDILDVAKIESGHLTLTPErvrlrhvV 328
Cdd:PRK10815 270 LTDLTHSLKTPL-AV---LQSTLRSLRSGKQmsvEQAE-PIMLEQISRISQQIGYYLHRASMRSEHNLLSRE-------L 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  329 ESVRRMFEGLA-------RQKGLrlVVELDDAPGRDVLIDPLRFKQVLSNLVSNAIKFT-ERGQVTIRLQERSLdegrai 400
Cdd:PRK10815 338 HSVAPLLDNLTsalnkvyQRKGV--NITLDISPEITFVGEKNDFMEVMGNVLDNACKYClEFVEISARQTDEHL------ 409

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  401 vRVDVEDSGIGIAPADQARLFQpfiqvaKGR---TVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRV 467
Cdd:PRK10815 410 -HIVVEDDGPGIPESKRELIFD------RGQradTLRPGQGLGLSVAREITEQYEGKISAGDSPLGGARM 472

HATPase_CheA-like

cd16916

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...

327-471

2.12e-04

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

Pssm-ID: 340393 [Multi-domain] Cd Length: 178 Bit Score: 42.57 E-value: 2.12e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 327 VVESVRRMFEGLAR--QKGLRLVVElddapGRDVLIDplrfKQVLSN-------LVSNAI-------------KFTERGQ 384
Cdd:cd16916   1 VFSRFPRLVRDLARelGKQVELVVE-----GEDTELD----KSVLEKladplthLLRNAVdhgieapeerlaaGKPPEGT 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 385 VTIRLQERSldeGRAIVRVdvEDSGIGIAP--------------ADQAR----------LFQPFIQVAKGRTVQGGTGLG 440
Cdd:cd16916  72 ITLRAEHQG---NQVVIEV--SDDGRGIDRekirekaierglitADEAAtlsddevlnlIFAPGFSTAEQVTDVSGRGVG 146

                       170       180       190
                ....*....|....*....|....*....|.
gi 15598240 441 LAICRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16916 147 MDVVKRSIESLGGTIEVESEPGQGTTFTIRL 177

PRK11517

DNA-binding response regulator HprR;

498-610

2.13e-04

DNA-binding response regulator HprR;

Pssm-ID: 183172 [Multi-domain] Cd Length: 223 Bit Score: 43.35 E-value: 2.13e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  498 LHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQerceRRAPILI 577
Cdd:PRK11517   1 MKILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTA----KQTPVIC 76

                         90       100       110
                 ....*....|....*....|....*....|...
gi 15598240  578 LgyTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:PRK11517  77 L--TARDSVDDRVRGLDSGANDYLVKPFSFSEL 107

PAS

pfam00989

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...

112-224

2.55e-04

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

Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 41.25 E-value: 2.55e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240   112 ALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQCLAVARGGTASFTDMAV 191
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFR 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15598240   192 RIGGQLLEIHHWVTPYRDRQGRVLGLMNGWIDI 224
Cdd:pfam00989  81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113

HATPase_EL346-LOV-HK-like

cd16951

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

368-471

3.84e-04

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

Pssm-ID: 340427 [Multi-domain] Cd Length: 131 Bit Score: 40.86 E-value: 3.84e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 368 VLSNLVSNAIK--FTER--GQVTIRLQErsldeGRAIVRVDVEDSGIGIApadqarlfQPFIQVAKGRtvqggtgLGLAI 443
Cdd:cd16951  43 VVNELLQNALKhaFSDRegGTITIRSVV-----DGDYLRITVIDDGVGLP--------QDEDWPNKGS-------LGLQI 102

                        90       100
                ....*....|....*....|....*...
gi 15598240 444 CRKLVDLMGGDVEMHSEPGKGTRVSLDL 471
Cdd:cd16951 103 VRSLVEGELKAFLEVQSAENGTRVNIDI 130

REC_OmpR_VirG

cd17594

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...

499-610

5.52e-04

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: 40.12 E-value: 5.52e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerRAPILIL 578
Cdd:cd17594   1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARS----DVPIIII 76

                        90       100       110
                ....*....|....*....|....*....|..
gi 15598240 579 GYTADAEPDEVQrCRDAGMDDCLFKPLGLETL 610
Cdd:cd17594  77 SGDRRDEIDRVV-GLELGADDYLAKPFGLREL 107

REC_OmpR_ChvI-like

cd19936

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...

500-604

6.16e-04

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: 39.74 E-value: 6.16e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerraPILILG 579
Cdd:cd19936   1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKSTL----PVIFLT 76

                        90       100
                ....*....|....*....|....*
gi 15598240 580 yTADAEPDEVQRCRdAGMDDCLFKP 604
Cdd:cd19936  77 -SKDDEIDEVFGLR-MGADDYITKP 99

PRK10365

sigma-54-dependent response regulator transcription factor ZraR;

495-618

6.39e-04

sigma-54-dependent response regulator transcription factor ZraR;

Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 42.71 E-value: 6.39e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  495 SRRLHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCerrAP 574
Cdd:PRK10365   3 HDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA---IP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15598240  575 ILILgyTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYLATSF 618
Cdd:PRK10365  80 VLIM--TAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121

PRK10816

two-component system response regulator PhoP;

498-608

7.50e-04

two-component system response regulator PhoP;

Pssm-ID: 182755 [Multi-domain] Cd Length: 223 Bit Score: 41.65 E-value: 7.50e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  498 LHILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPILI 577
Cdd:PRK10816   1 MRVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSN---DVSLPILV 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15598240  578 LgyTADAEPDEVQRCRDAGMDDCLFKPLGLE 608
Cdd:PRK10816  78 L--TARESWQDKVEVLSAGADDYVTKPFHIE 106

glnG

PRK10923

nitrogen regulation protein NR(I); Provisional

500-642

7.77e-04

nitrogen regulation protein NR(I); Provisional

Pssm-ID: 182842 [Multi-domain] Cd Length: 469 Bit Score: 42.55 E-value: 7.77e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercERRAPILILg 579
Cdd:PRK10923   6 VWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQR---HPMLPVIIM- 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15598240  580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETLRNYL--ATSFGRDAAQPRGLYDAAALSSLGGDRP 642
Cdd:PRK10923  82 -TAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVerAISHYQEQQQPRNIQVNGPTTDIIGEAP 145

REC_RegA-like

cd17563

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...

499-580

7.80e-04

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: 39.73 E-value: 7.80e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIR-IQERCErrapILI 577
Cdd:cd17563   2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRaLQPDAR----IVV 77


                ....
gi 15598240 578 L-GY 580
Cdd:cd17563  78 LtGY 81

REC_OmpR_CtrA

cd17616

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...

500-610

7.96e-04

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: 39.70 E-value: 7.96e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIqerCERRAPILILG 579
Cdd:cd17616   1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRL---AKVKTPILILS 77

                        90       100       110
                ....*....|....*....|....*....|.
gi 15598240 580 YTADAEpDEVqRCRDAGMDDCLFKPLGLETL 610
Cdd:cd17616  78 GLADIE-DKV-KGLGFGADDYMTKPFHKDEL 106

REC_DesR-like

cd19930

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...

500-603

8.61e-04

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

Pssm-ID: 381157 [Multi-domain] Cd Length: 117 Bit Score: 39.56 E-value: 8.61e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLG--HRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCERRAPILi 577
Cdd:cd19930   1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR-EELPDTKVLIV- 78

                        90       100
                ....*....|....*....|....*.
gi 15598240 578 lgyTADAEPDEVQRCRDAGMDDCLFK 603
Cdd:cd19930  79 ---TTFGRPGYFRRALAAGVDGYVLK 101

REC_NarL

cd19931

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...

500-610

1.25e-03

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381158 [Multi-domain] Cd Length: 117 Bit Score: 39.25 E-value: 1.25e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGH--RVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCERRAPILI 577
Cdd:cd19931   1 VLLIDDHPLLRKGIKQLIELDPDftVVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALR-EEGVSARIVILT 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 15598240 578 LgytADAEPDeVQRCRDAGMDDCLFKPLGLETL 610
Cdd:cd19931  80 V---SDAEDD-VVTALRAGADGYLLKDMEPEDL 108

HATPase_PDK-like

cd16929

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...

403-471

1.31e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.

Pssm-ID: 340406 [Multi-domain] Cd Length: 169 Bit Score: 40.40 E-value: 1.31e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 403 VDVEDSGIGIAPADQARLF--------QPFIQV------AKGRTVQGGTGLGLAICRKLVDLMGGDVEMHSEPGKGTRVS 468
Cdd:cd16929  86 IKISDRGGGIPREDLARLFsymystapQPSLDDfsdlisGTQPSPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVY 165


                ...
gi 15598240 469 LDL 471
Cdd:cd16929 166 IYL 168

PAS

COG2202

PAS domain [Signal transduction mechanisms];

102-234

1.39e-03

PAS domain [Signal transduction mechanisms];

Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 41.16 E-value: 1.39e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 102 RTEADLSGRLALKQALVDGIPYPVSIRTLDGRLLACNRNYLESLRMTREQARGTLLTDSDWVEGSKARLMHQQCLAVARG 181
Cdd:COG2202 127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGR 206

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15598240 182 GTASFTDMAVRIGGQLLEIHHWVTPYRDRQGRVLGLMNGwIDITERERLARQL 234
Cdd:COG2202 207 ESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIV-RDITERKRAEEAL 258

psREC_PRR

cd17582

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...

500-604

1.93e-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: 38.54 E-value: 1.93e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEV--LISDCNMPRLNGYQLARRIRIQERCeRRAPILI 577
Cdd:cd17582   1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIdlILTEVDLPVSSGFKLLSYIMRHKIC-KNIPVIM 79

                        90       100
                ....*....|....*....|....*..
gi 15598240 578 LgyTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17582  80 M--SSQDSVGVVFKCLSKGAADYLVKP 104

REC_Spo0A

cd17561

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...

497-604

1.95e-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: 38.36 E-value: 1.95e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 497 RLHILIADDyppNRVLLRQQLEFLGHR-----VAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCER 571
Cdd:cd17561   1 KIKVLIADD---NREFVQLLEEYLNSQpdmevVGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLR-RMRLEK 76

                        90       100       110
                ....*....|....*....|....*....|...
gi 15598240 572 RAPILILgyTADAEPDEVQRCRDAGMDDCLFKP 604
Cdd:cd17561  77 RPKIIML--TAFGQEDITQRAVELGASYYILKP 107

HATPase_YpdA-like

cd16955

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...

366-468

2.13e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.

Pssm-ID: 340431 [Multi-domain] Cd Length: 102 Bit Score: 38.21 E-value: 2.13e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 366 KQVLSNLVSNAIK---FTERGQVTIRLQERSLDEGRaiVRVDVEDSGIGIAPADQARLFQPFIQvakgrtvqgGTGLGLA 442
Cdd:cd16955   3 KLMIQPLVENAIVhgiQEKKGKGVVKISVKKQLKNR--LHIAVEDNGIGISPKVIERVEQDEMP---------GNKIGLL 71

                        90       100
                ....*....|....*....|....*...
gi 15598240 443 ICRKLVDLMGGDvEMH--SEPGKGTRVS 468
Cdd:cd16955  72 NVHQRLKLGYGE-GLHirSRPDPGTLIA 98

CheA

COG0643

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];

271-471

3.51e-03

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];

Pssm-ID: 440408 [Multi-domain] Cd Length: 563 Bit Score: 40.55 E-value: 3.51e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 271 ELVLQRLAPEQR----ERASLEVAYEAAGSLQLLIGDILDVAKiesgHLTLTPervrLRHVVESVRRMFEGLARQ--KGL 344
Cdd:COG0643 188 ELVITRARLEQLaeelEDESLRELEEALEQLSRLTRELQDGVM----RLRMVP----ISTVFNRFPRMVRDLARElgKEV 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 345 RLVVElddapGRDVLIDplrfKQVLSN-------LVSNAI--------------KfTERGQVTIRLQErsldEGRAIVrV 403
Cdd:COG0643 260 ELVIE-----GEETELD----RTVLERlgdplvhLVRNAVdhgietpeerlaagK-PETGTITLSAYH----EGGRVV-I 324

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 404 DVEDSGIGI---------------APADQARL---------FQP-FIQVAK-----GRtvqggtGLGLAICRKLVDLMGG 453
Cdd:COG0643 325 EVSDDGRGLdlekirakaiekgliTAEEAAALsdeelleliFAPgFSTAEEvtdlsGR------GVGMDVVKTNIEALGG 398

                       250
                ....*....|....*...
gi 15598240 454 DVEMHSEPGKGTRVSLDL 471
Cdd:COG0643 399 TIEIESEPGKGTTFTLRL 416

PRK10403

nitrate/nitrite response regulator protein NarP;

499-603

4.14e-03

nitrate/nitrite response regulator protein NarP;

Pssm-ID: 182431 [Multi-domain] Cd Length: 215 Bit Score: 39.45 E-value: 4.14e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  499 HILIADDYPPNRVLLRQQLEF--LGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQERCERrapIL 576
Cdd:PRK10403   8 QVLIVDDHPLMRRGVRQLLELdpGFEVVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVTAQ---II 84

                         90       100
                 ....*....|....*....|....*..
gi 15598240  577 ILgyTADAEPDEVQRCRDAGMDDCLFK 603
Cdd:PRK10403  85 IL--TVSDASSDVFALIDAGADGYLLK 109

fixJ

PRK09390

response regulator FixJ; Provisional

495-634

5.13e-03

response regulator FixJ; Provisional

Pssm-ID: 181815 [Multi-domain] Cd Length: 202 Bit Score: 38.83 E-value: 5.13e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  495 SRRLHILIADDYPPnrvlLRQQLEFL----GHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQercE 570
Cdd:PRK09390   1 SDKGVVHVVDDDEA----MRDSLAFLldsaGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLKAR---G 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15598240  571 RRAPILILGYTADAePDEVQRCRdAGMDDCLFKPLGLETLRNYLATSFGRDAAQPRGLYDAAAL 634
Cdd:PRK09390  74 SPLPVIVMTGHGDV-PLAVEAMK-LGAVDFIEKPFEDERLIGAIERALAQAPEAAKSEAVAADI 135

PRK10161

phosphate response regulator transcription factor PhoB;

500-610

6.08e-03

phosphate response regulator transcription factor PhoB;

Pssm-ID: 182277 [Multi-domain] Cd Length: 229 Bit Score: 38.93 E-value: 6.08e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240  500 ILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRiQERCERRAPILILg 579
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLK-RESMTRDIPVVML- 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15598240  580 yTADAEPDEVQRCRDAGMDDCLFKPLGLETL 610
Cdd:PRK10161  83 -TARGEEEDRVRGLETGADDYITKPFSPKEL 112

PRK04184

DNA topoisomerase VI subunit B; Validated

367-421

6.30e-03

DNA topoisomerase VI subunit B; Validated

Pssm-ID: 235246 [Multi-domain] Cd Length: 535 Bit Score: 39.88 E-value: 6.30e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15598240  367 QVLSNLVSNAIKFTERGQV--TIRLQERSLDEGRAIVRVDVEDSGIGIAPADQARLF 421
Cdd:PRK04184  39 TTVKELVDNSLDACEEAGIlpDIKIEIKRVDEGKDHYRVTVEDNGPGIPPEEIPKVF 95

REC_OmpR_BfmR-like

cd19939

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...

499-604

7.12e-03

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.

Pssm-ID: 381166 [Multi-domain] Cd Length: 116 Bit Score: 36.97 E-value: 7.12e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15598240 499 HILIADDYPPNRVLLRQQLEFLGHRVAEAEDGQVALELWADERFEVLISDCNMPRLNGYQLARRIRIQErcerRAPILIL 578
Cdd:cd19939   1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS----HVPILML 76

                        90       100
                ....*....|....*....|....*...
gi 15598240 579 gytaDAEPDEVQRCR--DAGMDDCLFKP 604
Cdd:cd19939  77 ----TARTEEMDRVLglEMGADDYLCKP 100

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