NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|794205150|gb|AKA51141|]
View 

histidine kinase [Bacteroides fragilis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
225-495 4.62e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


:

Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 248.67  E-value: 4.62e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 225 EIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDRMRRSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFS 304
Cdd:COG0642   53 LLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 305 EIIALTEDEkEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRP 383
Cdd:COG0642  133 ELLLEELDE-EQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVvELFRPLAEEKGIELELDLP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 384 SEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL--NDFVQGT 460
Cdd:COG0642  212 DDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTdpSRRGGGT 291
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 794205150 461 GLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG0642  292 GLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
516-635 6.55e-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: 125.73  E-value: 6.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 516 VENRQKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQ--EI 592
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRlpDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 794205150 593 PIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
PAS super family cl43642
PAS domain [Signal transduction mechanisms];
54-268 2.99e-08

PAS domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG2202:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.03  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  54 ILGLKEAGIIFRDINDFYrfaHPEDVISYQTTFARMLESEtKISQIVVRCVGRQGETIWLEDNFIAYKkNKENGSDKIIA 133
Cdd:COG2202   43 LTGYSAEELLGKTLRDLL---PPEDDDEFLELLRAALAGG-GVWRGELRNRRKDGSLFWVELSISPVR-DEDGEITGFVG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 134 YTANITSRCEKEAQIRQLEERNRKIIEALPEFIFIFDDNFFITDVLMAPDTELLHPVEVLKGADGRSIYSSEVSDLFISS 213
Cdd:COG2202  118 IARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 794205150 214 IHECLKSG-KLKEIEYPV-DVEAGRHFFQARIAPFEGNK----VLALIHDIGDRMRRSQEL 268
Cdd:COG2202  198 LRRLLEGGrESYELELRLkDGDGRWVWVEASAVPLRDGGevigVLGIVRDITERKRAEEAL 258
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
225-495 4.62e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 248.67  E-value: 4.62e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 225 EIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDRMRRSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFS 304
Cdd:COG0642   53 LLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 305 EIIALTEDEkEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRP 383
Cdd:COG0642  133 ELLLEELDE-EQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVvELFRPLAEEKGIELELDLP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 384 SEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL--NDFVQGT 460
Cdd:COG0642  212 DDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTdpSRRGGGT 291
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 794205150 461 GLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG0642  292 GLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
263-635 2.19e-71

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 248.54  E-value: 2.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  263 RRSQELLE---AKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILD 339
Cdd:TIGR02956 442 RLNAEVKNhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILD 521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  340 LSRIESGKSEMHCQLTEMSGLVDEVdkVHRLKMK---KGVKLNVIRPSE-EIWISTDRNRVTQVLFNFLSNAIKNTIEGS 415
Cdd:TIGR02956 522 YSKIEAGHLSISPRPFDLNALLDDV--HHLMVSRaqlKGIQLRLNIPEQlPNWWQGDGPRIRQVLINLVGNAIKFTDRGS 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  416 ITFGL-VKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLND--FVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFIL 492
Cdd:TIGR02956 600 VVLRVsLNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGrrRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWF 679
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  493 YLPNRQVQEVvvgerENAAGNMGVENRQKKILIAEDVESSYLQINAFL-KKEYTILWVPNGEEAVKSFIREKPDLILMDI 571
Cdd:TIGR02956 680 TLPLTRGKPA-----EDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLtRLGHKVTLAESGQSALECFHQHAFDLALLDI 754
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 794205150  572 RMPVMNGIQATAKIRAI---SQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:TIGR02956 755 NLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
PRK15347 PRK15347
two component system sensor kinase;
264-633 3.38e-65

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 230.68  E-value: 3.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 264 RSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRI 343
Cdd:PRK15347 380 RTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRI 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 344 ESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNV-IRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSITFGLV 421
Cdd:PRK15347 460 ESGQMTLSLEETALLPLLDQAmLTIQGPAQSKSLTLRTfVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVK 539
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 422 KEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFIL--------- 492
Cdd:PRK15347 540 RHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLvlplneyap 619
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 493 ----------------------------------------YLPNR---QVQEVVVGERENAAGNMGVENRQKKILIAEDV 529
Cdd:PRK15347 620 peplkgelsaplalhrqlsawgitcqpghqnpalldpelaYLPGRlydLLQQIIQGAPNEPVINLPLQPWQLQILLVDDV 699
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 530 ESSYLQINAFL----KKEYTilwVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIR----AISQEIPIIAITAYA 601
Cdd:PRK15347 700 ETNRDIIGMMLvelgQQVTT---AASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRddpnNLDPDCMIVALTANA 776
                        410       420       430
                 ....*....|....*....|....*....|..
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:PRK15347 777 APEEIHRCKKAGMNHYLTKPVTLAQLARALEL 808
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
253-495 6.47e-44

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 166.08  E-value: 6.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 253 ALIHDIGDrmrrsQELLEAKQRAeeadrmksvFLANMSHEIRTPLNAIVGFSEiiALTE----DEKEKEEYLGIIQQNSN 328
Cdd:NF033092 357 AVLHDVTE-----QEKIEQERRE---------FVANVSHELRTPLTTMRSYLE--ALADgawkDPELAPRFLGVTQNETE 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 329 LLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEVdkVHRLKM---KKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLS 405
Cdd:NF033092 421 RMIRLVNDLLQLSRMDSKDYKLNKEWVNFNEFFNYI--IDRFEMilkNKNITFKREFPKRDLWVEIDTDKITQVLDNIIS 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 406 NAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF--------EKLNdfvqGTGLGLPICKSIVERLGG 476
Cdd:NF033092 499 NAIKYSPEgGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFyrvdkarsRKMG----GTGLGLAIAKEVVEAHGG 574
                        250
                 ....*....|....*....
gi 794205150 477 RIEVESELGQGSTFILYLP 495
Cdd:NF033092 575 RIWAESEEGKGTTIYFTLP 593
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
398-495 5.31e-34

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: 125.30  E-value: 5.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNTIEGSITF-----GLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFV----QGTGLGLPICK 468
Cdd:cd16922    3 QILLNLLGNAIKFTEEGEVTLrvsleEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTtrkyGGTGLGLAISK 82
                         90       100
                 ....*....|....*....|....*..
gi 794205150 469 SIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16922   83 KLVELMGGDISVESEPGQGSTFTFTLP 109
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
516-635 6.55e-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: 125.73  E-value: 6.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 516 VENRQKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQ--EI 592
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRlpDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 794205150 593 PIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
391-495 9.39e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.60  E-value: 9.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150   391 TDRNRVTQVLFNFLSNAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF---EKLNDFVQGTGLGLPI 466
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFfrtDKRSRKIGGTGLGLSI 80
                           90       100
                   ....*....|....*....|....*....
gi 794205150   467 CKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
523-631 2.88e-30

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: 114.87  E-value: 2.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA---ISQEIPIIAIT 598
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
391-495 1.15e-28

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: 110.15  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  391 TDRNRVTQVLFNFLSNAIK-NTIEGSITFGlVKEEEWVKLYVTDTGCGISKEKLPLIFTRF-EKLNDFVQGTGLGLPICK 468
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKhAAKAGEITVT-LSEGGELTLTVEDNGIGIPPEDLPRIFEPFsTADKRGGGGTGLGLSIVR 79
                          90       100
                  ....*....|....*....|....*..
gi 794205150  469 SIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:pfam02518  80 KLVELLGGTITVESEPGGGTTVTLTLP 106
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
523-632 1.59e-25

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: 101.46  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 794205150  602 FCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
273-497 2.24e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 110.11  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 273 QRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEkekeeyLGIIQQNSNLLLQ--------LINDILDLSRIE 344
Cdd:NF040691 262 RQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDD------FDPATARSAELLHteldrfesLLSDLLEISRFD 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 345 SGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTiEGS---ITFGl 420
Cdd:NF040691 336 AGAAELDVEPVDLRPLVRRVvDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKpvvVTVA- 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 421 vKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPN 496
Cdd:NF040691 414 -QDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdparARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPR 492

                 .
gi 794205150 497 R 497
Cdd:NF040691 493 V 493
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
239-495 9.48e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 95.66  E-value: 9.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 239 FQARIAPFEGNKVLALIHDigdrMRRSQELLEAKQRaeeadrMKSVFLANMSHEIRTPLNAIVGFSEIIaltED--EKEK 316
Cdd:NF012163 207 YTTRVTPTSNDELGKLAQD----FNQLASTLEKNEQ------MRRDFMADISHELRTPLAVLRAELEAI---QDgiRKFT 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 317 EEYLGIIQQNSNLLLQLINDILDLSRIESGksEMHCQLTEMS--GLVDEVDKVHRLKM-KKGVKLNVIRPsEEIWISTDR 393
Cdd:NF012163 274 PESLDSLQAEVGTLTKLVDDLHDLSMSDEG--ALAYQKASVDlvPLLEVEGGAFRERFaSAGLELEVSLP-DSSLVFGDR 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 394 NRVTQVLFNFLSNAIKNT-IEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPICK 468
Cdd:NF012163 351 DRLMQLFNNLLENSLRYTdSGGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVevsrNRASGGSGLGLAISL 430
                        250       260
                 ....*....|....*....|....*...
gi 794205150 469 SIVERLGGRIEVE-SELGqGSTFILYLP 495
Cdd:NF012163 431 NIVQAHGGTLHAAhSPLG-GLRIVVTLP 457
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
522-628 4.19e-18

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 87.21  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAY 600
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100
                 ....*....|....*....|....*...
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYPLEKLK 628
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELN 113
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
521-574 5.52e-09

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: 52.19  E-value: 5.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 794205150   521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMP 574
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PAS COG2202
PAS domain [Signal transduction mechanisms];
54-268 2.99e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.03  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  54 ILGLKEAGIIFRDINDFYrfaHPEDVISYQTTFARMLESEtKISQIVVRCVGRQGETIWLEDNFIAYKkNKENGSDKIIA 133
Cdd:COG2202   43 LTGYSAEELLGKTLRDLL---PPEDDDEFLELLRAALAGG-GVWRGELRNRRKDGSLFWVELSISPVR-DEDGEITGFVG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 134 YTANITSRCEKEAQIRQLEERNRKIIEALPEFIFIFDDNFFITDVLMAPDTELLHPVEVLKGADGRSIYSSEVSDLFISS 213
Cdd:COG2202  118 IARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 794205150 214 IHECLKSG-KLKEIEYPV-DVEAGRHFFQARIAPFEGNK----VLALIHDIGDRMRRSQEL 268
Cdd:COG2202  198 LRRLLEGGrESYELELRLkDGDGRWVWVEASAVPLRDGGevigVLGIVRDITERKRAEEAL 258
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
49-134 3.68e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 39.63  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150   49 DEYFHILGLKEAGIIfRDINDFYRFAHPEDVISYQTTFARMLESETKISqIVVRCVGRQGETIWLEDNFIAYkKNKENGS 128
Cdd:pfam08447   6 PRFEEILGYTPEELL-GKGESWLDLVHPDDRERVREALWEALKGGEPYS-GEYRIRRKDGEYRWVEARARPI-RDENGKP 82

                  ....*.
gi 794205150  129 DKIIAY 134
Cdd:pfam08447  83 VRVIGV 88
 
Name Accession Description Interval E-value
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
225-495 4.62e-77

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 248.67  E-value: 4.62e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 225 EIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDRMRRSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFS 304
Cdd:COG0642   53 LLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 305 EIIALTEDEkEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRP 383
Cdd:COG0642  133 ELLLEELDE-EQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVvELFRPLAEEKGIELELDLP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 384 SEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL--NDFVQGT 460
Cdd:COG0642  212 DDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGtVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTdpSRRGGGT 291
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 794205150 461 GLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG0642  292 GLGLAIVKRIVELHGGTIEVESEPGKGTTFTVTLP 326
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
267-498 1.27e-74

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 239.04  E-value: 1.27e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 267 ELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIA--LTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIE 344
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLdeEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 345 SGKSEMHCQLTEMSGLVDE-VDKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVK 422
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEaVEELRPLAEEKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGtITISARR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 794205150 423 EEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDF--VQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQ 498
Cdd:COG2205  161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSrgEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
225-498 6.08e-72

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 237.14  E-value: 6.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 225 EIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDRMRRSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFS 304
Cdd:COG5002  108 LALLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYL 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 305 EII--ALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVI 381
Cdd:COG5002  188 ELLldGAADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVvEELRPLAEEKGIELELD 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 382 RPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDF 456
Cdd:COG5002  268 LPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGtITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVdksrSRE 347
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 794205150 457 VQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQ 498
Cdd:COG5002  348 TGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLAR 389
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
263-635 2.19e-71

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 248.54  E-value: 2.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  263 RRSQELLE---AKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILD 339
Cdd:TIGR02956 442 RLNAEVKNhakARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILD 521
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  340 LSRIESGKSEMHCQLTEMSGLVDEVdkVHRLKMK---KGVKLNVIRPSE-EIWISTDRNRVTQVLFNFLSNAIKNTIEGS 415
Cdd:TIGR02956 522 YSKIEAGHLSISPRPFDLNALLDDV--HHLMVSRaqlKGIQLRLNIPEQlPNWWQGDGPRIRQVLINLVGNAIKFTDRGS 599
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  416 ITFGL-VKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLND--FVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFIL 492
Cdd:TIGR02956 600 VVLRVsLNDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGrrRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWF 679
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  493 YLPNRQVQEVvvgerENAAGNMGVENRQKKILIAEDVESSYLQINAFL-KKEYTILWVPNGEEAVKSFIREKPDLILMDI 571
Cdd:TIGR02956 680 TLPLTRGKPA-----EDSATLTVIDLPPQRVLLVEDNEVNQMVAQGFLtRLGHKVTLAESGQSALECFHQHAFDLALLDI 754
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 794205150  572 RMPVMNGIQATAKIRAI---SQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:TIGR02956 755 NLPDGDGVTLLQQLRAIygaKNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVIL 821
PRK15347 PRK15347
two component system sensor kinase;
264-633 3.38e-65

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 230.68  E-value: 3.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 264 RSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRI 343
Cdd:PRK15347 380 RTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRI 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 344 ESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNV-IRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSITFGLV 421
Cdd:PRK15347 460 ESGQMTLSLEETALLPLLDQAmLTIQGPAQSKSLTLRTfVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGGIRLRVK 539
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 422 KEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFIL--------- 492
Cdd:PRK15347 540 RHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLvlplneyap 619
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 493 ----------------------------------------YLPNR---QVQEVVVGERENAAGNMGVENRQKKILIAEDV 529
Cdd:PRK15347 620 peplkgelsaplalhrqlsawgitcqpghqnpalldpelaYLPGRlydLLQQIIQGAPNEPVINLPLQPWQLQILLVDDV 699
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 530 ESSYLQINAFL----KKEYTilwVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIR----AISQEIPIIAITAYA 601
Cdd:PRK15347 700 ETNRDIIGMMLvelgQQVTT---AASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRddpnNLDPDCMIVALTANA 776
                        410       420       430
                 ....*....|....*....|....*....|..
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:PRK15347 777 APEEIHRCKKAGMNHYLTKPVTLAQLARALEL 808
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
201-634 7.67e-59

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 210.95  E-value: 7.67e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 201 IYSSEVSDLFISSIHECLKSGKLKEIEYPVDVEAGR-HFFQARIAPF--EGNKVLALI---HDIGDRmRRSQELLEakqr 274
Cdd:PRK11091 203 VYSPEAAEKVIETDEKVFRHNVSLTYEQWLDYPDGRkACFELRKVPFydRVGKRHGLMgfgRDITER-KRYQDALE---- 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 275 aeEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQL 354
Cdd:PRK11091 278 --KASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQP 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 355 TEMSGLVDEVDKVHRLKMK-KGVKLNV-IRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSITFGLVKEEEWVKLY-V 431
Cdd:PRK11091 356 IDFTDFLADLENLSGLQAEqKGLRFDLePLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRVRYEEGDMLTFeV 435
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 432 TDTGCGISKEKLPLIFTRFEKLND-----FVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQVQEVVVGE 506
Cdd:PRK11091 436 EDSGIGIPEDELDKIFAMYYQVKDshggkPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEEVEDA 515
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 507 RENAAgnmgVENRQKKILIAEDVESSYLQINAFLKK-EYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKI 585
Cdd:PRK11091 516 FDEDD----MPLPALNILLVEDIELNVIVARSVLEKlGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIAREL 591
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 794205150 586 RAIS---QEIPIIAITAYAFCPEGErALEAGCNEVIAKPYPLEKLKETIETY 634
Cdd:PRK11091 592 RERYpreDLPPLVALTANVLKDKKE-YLDAGMDDVLSKPLSVPALTAMIKKF 642
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
267-634 1.49e-50

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 188.52  E-value: 1.49e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 267 ELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESG 346
Cdd:PRK11107 278 ELDLAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAG 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 347 KSE---MHCQLTEMsglVDEVdkVHRLK---MKKGVKLNV-IRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSITFG 419
Cdd:PRK11107 358 KLVlenIPFSLRET---LDEV--VTLLAhsaHEKGLELTLnIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDIL 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 420 LVK---EEEWVKL--YVTDTGCGISKEKLPLIFTRFEklndfvQ----------GTGLGLPICKSIVERLGGRIEVESEL 484
Cdd:PRK11107 433 VELralSNTKVQLevQIRDTGIGISERQQSQLFQAFR------QadasisrrhgGTGLGLVITQKLVNEMGGDISFHSQP 506
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 485 GQGSTF--------------------------ILYL-PNRQVQEVVvgERENAAGNMGVENRQ----------KKILIAE 527
Cdd:PRK11107 507 NRGSTFwfhlpldlnpnpiidglptdclagkrLLYVePNSAAAQAT--LDILSETPLEVTYSPtlsqlpeahyDILLLGL 584
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 528 DVESSY------LQINAFLKK-EYTILWVP-------------------------------------------------- 550
Cdd:PRK11107 585 PVTFREpltmlhERLAKAKSMtDFLILALPcheqvlaeqlkqdgadaclskplshtrllpallepchhkqppllpptdes 664
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 ----------------------------------NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPI 594
Cdd:PRK11107 665 rlpltvmavddnpanlkligalleeqvehvvlcdSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPhnQNTPI 744
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 794205150 595 IAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETY 634
Cdd:PRK11107 745 IAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
47-498 1.21e-49

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 180.37  E-value: 1.21e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  47 FTDEYFHILGLKEAGIIFRDINDFYRFAHPEDVISYQTTFARMLESETKISQIVVRCVGRQGETIWLEDNFIAYKKNKEN 126
Cdd:COG4251   42 VLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 127 GSDKIIAYTANITSRCEKEAQIRQLEERNRKIIEALPEFIFIFDDNFFITDVLMAPDTELLHPVEVLKGADGRSIYSSEV 206
Cdd:COG4251  122 LLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLL 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 207 SDLFISSIHECLKSGKLKEIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDR-----MRRSQELLEAKQRAEEADRM 281
Cdd:COG4251  202 LLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLElrlelEELEEELEERTAELERSNEE 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 282 KSVFLANMSHEIRTPLNAIVGFSEIiaLTEDEKEK-----EEYLGIIQQNSNLLLQLINDILDLSRIesGKSEMHCQLTE 356
Cdd:COG4251  282 LEQFAYVASHDLREPLRKISGFSQL--LEEDYGDKldeegREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVD 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 357 MSGLVDEVDKVHRLKMK-KGVKLNVirpSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS---ITFGLVKEEEWVKLYVT 432
Cdd:COG4251  358 LNELLEEVLEDLEPRIEeRGAEIEV---GPLPTVRGDPTLLRQVFQNLISNAIKYSRPGEpprIEIGAEREGGEWVFSVR 434
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 794205150 433 DTGCGISKEKLPLIFTRFEKLN--DFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQ 498
Cdd:COG4251  435 DNGIGIDPEYAEKIFEIFQRLHsrDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAP 502
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
225-495 1.41e-49

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 176.53  E-value: 1.41e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 225 EIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGDRMRRSQELLEAKQRAEEADRMKSV--FLANMSHEIRTPLNAIVG 302
Cdd:COG4191   83 GLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALgeLAAGIAHEINNPLAAILG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 303 FSEIIA-LTEDEKEKE---EYLGIIQQNSNLLLQLINDILDLSRiesgKSEMHCQLTEMSGLVDEVDKV--HRLKmKKGV 376
Cdd:COG4191  163 NAELLRrRLEDEPDPEelrEALERILEGAERAAEIVRSLRAFSR----RDEEEREPVDLNELIDEALELlrPRLK-ARGI 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 377 KLNVIRPSEEIWISTDRNRVTQVLFNFLSNAI---KNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIF-----T 448
Cdd:COG4191  238 EVELDLPPDLPPVLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFepfftT 317
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 794205150 449 RFEKlndfvQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG4191  318 KPVG-----KGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLP 359
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
70-502 4.70e-49

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: 178.24  E-value: 4.70e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  70 FYRFAHPEDVISYQTTFARMLESETKiSQIVVRCVGRQGETIWlednFIAYKKNKENGSDKIIAYTA---NITSRCEKEA 146
Cdd:COG5809   60 ILDFLHPDDEKELREILKLLKEGESR-DELEFELRHKNGKRLE----FSSKLSPIFDQNGDIEGMLAisrDITERKRMEE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 147 QIRQLEERNRKIIEALPEFIfifddnffitdVLMAPDTELLH-----------PVEVLKGADGRSIYSSEVSDLFISSIH 215
Cdd:COG5809  135 ALRESEEKFRLIFNHSPDGI-----------IVTDLDGRIIYanpaackllgiSIEELIGKSILELIHSDDQENVAAFIS 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 216 ECLKSGKLKEIEYPVDVEAGRHF-FQARIAPF----EGNKVLALIHDIGDRmRRSQELLEAKQRAEEADRMksvfLANMS 290
Cdd:COG5809  204 QLLKDGGIAQGEVRFWTKDGRWRlLEASGAPIkkngEVDGIVIIFRDITER-KKLEELLRKSEKLSVVGEL----AAGIA 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 291 HEIRTPLNAIVGFSEIIALTEDEKEKEeYLGIIQQNSNLLLQLINDILDLSRIESGKSEMhcqlTEMSGLVDEV-DKVHR 369
Cdd:COG5809  279 HEIRNPLTSLKGFIQLLKDTIDEEQKT-YLDIMLSELDRIESIISEFLVLAKPQAIKYEP----KDLNTLIEEViPLLQP 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 370 LKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIE-GSITFGL-VKEEEWVKLYVTDTGCGISKEKLPLIF 447
Cdd:COG5809  354 QALLKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEgGNITIETkAEDDDKVVISVTDEGCGIPEERLKKLG 433
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 794205150 448 TRF----EKlndfvqGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQVQEV 502
Cdd:COG5809  434 EPFyttkEK------GTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSITLPIKLSEQV 486
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
214-490 2.40e-47

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: 169.70  E-value: 2.40e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  214 IHECLKSGKLKEieyPVDVEAGRH---FFQARIAPFEGNKVLALIHDIgDRMRRsqelLEakqraeeadRMKSVFLANMS 290
Cdd:TIGR02966  60 FVEYLAAGRFSE---PLELPSPINserVLEIRIAPYGEEQKLLVARDV-TRLRR----LE---------QMRRDFVANVS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  291 HEIRTPLNAIVGFSEIIA--LTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKV 367
Cdd:TIGR02966 123 HELRTPLTVLRGYLETLAdgPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLrDEA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  368 HRLKMKKGVKLNVIrPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEG-SITFGLVKEEEWVKLYVTDTGCGISKEKLPLI 446
Cdd:TIGR02966 203 EALSQGKNHQITFE-IDGGVDVLGDEDELRSAFSNLVSNAIKYTPEGgTITVRWRRDGGGAEFSVTDTGIGIAPEHLPRL 281
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 794205150  447 FTRFEKLNDF----VQGTGLGLPICKSIVERLGGRIEVESELGQGSTF 490
Cdd:TIGR02966 282 TERFYRVDKSrsrdTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
147-495 1.54e-45

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 165.40  E-value: 1.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 147 QIRQLEERNRKIIEALPefififddnffitDVLMAPDTELL-----HPVEVLKGADGRSIYSSEVSDLF------ISSIH 215
Cdd:COG3852    1 ALRESEELLRAILDSLP-------------DAVIVLDADGRityvnPAAERLLGLSAEELLGRPLAELFpedsplRELLE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 216 ECLKSGK-LKEIEYPVDVEAGRHF-FQARIAPFEGNK----VLALIHDIGDRMRRSQELLEAkqraeeaDRMKSV--FLA 287
Cdd:COG3852   68 RALAEGQpVTEREVTLRRKDGEERpVDVSVSPLRDAEgeggVLLVLRDITERKRLERELRRA-------EKLAAVgeLAA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 288 NMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRiesgKSEMHCQLTEMSGLVDEVDKV 367
Cdd:COG3852  141 GLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSR----PRPPEREPVNLHEVLERVLEL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 368 HRLKMKKGVKLnVIRPSEEIW-ISTDRNRVTQVLFNFLSNAI-----KNTI------EGSITFGLVKEEEWVKLYVTDTG 435
Cdd:COG3852  217 LRAEAPKNIRI-VRDYDPSLPeVLGDPDQLIQVLLNLVRNAAeampeGGTItirtrvERQVTLGGLRPRLYVRIEVIDNG 295
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 794205150 436 CGISKEKLPLIF-----TRFEklndfvqGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG3852  296 PGIPEEILDRIFepfftTKEK-------GTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLP 353
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
253-495 6.47e-44

cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in Staphylococcus aureus (sp|Q2G2U4.1|WALK_STAA8). A shorter version, as found in Streptococcus pneumoniae, called WalK(Spn) or VicK, is not included. WalK is part of a two-component system and works with partner protein WalR.


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 166.08  E-value: 6.47e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 253 ALIHDIGDrmrrsQELLEAKQRAeeadrmksvFLANMSHEIRTPLNAIVGFSEiiALTE----DEKEKEEYLGIIQQNSN 328
Cdd:NF033092 357 AVLHDVTE-----QEKIEQERRE---------FVANVSHELRTPLTTMRSYLE--ALADgawkDPELAPRFLGVTQNETE 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 329 LLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEVdkVHRLKM---KKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLS 405
Cdd:NF033092 421 RMIRLVNDLLQLSRMDSKDYKLNKEWVNFNEFFNYI--IDRFEMilkNKNITFKREFPKRDLWVEIDTDKITQVLDNIIS 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 406 NAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF--------EKLNdfvqGTGLGLPICKSIVERLGG 476
Cdd:NF033092 499 NAIKYSPEgGTITFRLLETHNRIIISISDQGLGIPKKDLDKIFDRFyrvdkarsRKMG----GTGLGLAIAKEVVEAHGG 574
                        250
                 ....*....|....*....
gi 794205150 477 RIEVESELGQGSTFILYLP 495
Cdd:NF033092 575 RIWAESEEGKGTTIYFTLP 593
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
272-628 1.16e-42

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 165.68  E-value: 1.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  272 KQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKE-EYLGIIQQNSNLLLQLINDILDLSRIESGKSEM 350
Cdd:PRK09959  702 RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESGNYQL 781
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  351 HCQLTEMSGLV-DEVDKVHRLKMKKGVKLNVIRP-SEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS--ITFGLVKEEE- 425
Cdd:PRK09959  782 QPQWVDIPTLVqNTCHSFGAIAASKSIALSCSSTfPDHYLVKIDPQAFKQVLSNLLSNALKFTTEGAvkITTSLGHIDDn 861
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  426 --WVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQ--GTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNRQVQE 501
Cdd:PRK09959  862 haVIKMTIMDSGSGLSQEEQQQLFKRYSQTSAGRQqtGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQ 941
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  502 VVVGErenAAGNMGVENRQK-KILIAEDVESSYLqinaFLKKEYTILW-----VPNGEEAVKSFIREKPDLILMDIRMPV 575
Cdd:PRK09959  942 VATVE---AKAEQPITLPEKlSILIADDHPTNRL----LLKRQLNLLGydvdeATDGVQALHKVSMQHYDLLITDVNMPN 1014
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 794205150  576 MNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLK 628
Cdd:PRK09959 1015 MDGFELTRKLREQNSSLPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLK 1067
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
257-634 1.88e-41

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 161.68  E-value: 1.88e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 257 DIGDRMRRSQELLEAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLIND 336
Cdd:PRK10841 422 DVSARVKMEESLQEMAQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISD 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 337 ILDLSRIESGK-----SEMHCQ--LTEMSG----LVdevdkvhrlkMKKGVKLNV-IRPSEEIWISTDRNRVTQVLFNFL 404
Cdd:PRK10841 502 ILDFSKIESEQlkiepREFSPRevINHITAnylpLV----------VKKRLGLYCfIEPDVPVALNGDPMRLQQVISNLL 571
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 405 SNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFV----QGTGLGLPICKSIVERLGGRIEV 480
Cdd:PRK10841 572 SNAIKFTDTGCIVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVqrnfQGTGLGLAICEKLINMMDGDISV 651
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 481 ESELGQGSTFILYLPNRQVQEVVVGERENAAGN-----------------------MGVENRQKK------ILIAEDVES 531
Cdd:PRK10841 652 DSEPGMGSQFTIRIPLYGAQYPQKKGVEGLQGKrcwlavrnasleqfletllqrsgIQVQRYEGQeptpedVLITDDPVQ 731
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 532 SYLQINAF--------------------------------LKKEYTI-LWVPNGEEAVKSFIREK--------------P 564
Cdd:PRK10841 732 KKWQGRAVitfcrrhigipleiapgewvhstatphelpalLARIYRIeLESDDSANALPSTDKAVsdnddmmilvvddhP 811
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 565 -----------------------------------DLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERA 609
Cdd:PRK10841 812 inrrlladqlgslgyqcktandgvdalnvlsknhiDIVLTDVNMPNMDGYRLTQRLRQLGLTLPVIGVTANALAEEKQRC 891
                        490       500
                 ....*....|....*....|....*
gi 794205150 610 LEAGCNEVIAKPYPLEKLKETIETY 634
Cdd:PRK10841 892 LEAGMDSCLSKPVTLDVLKQTLTVY 916
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
198-495 3.91e-41

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: 154.73  E-value: 3.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 198 GRSIYSSEVSDLFISSIHECLKSGKLKEIEYPVDveaGRHFFQARIAPFEGNKVLALIHDIgdrmrrsQELLEAKqraee 277
Cdd:COG5000  132 GKPLEELLPELDLAELLREALERGWQEEIELTRD---GRRTLLVRASPLRDDGYVIVFDDI-------TELLRAE----- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 278 adRMKSV--FLANMSHEIRTPLNAIVGFSEIIA------LTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIesgkSE 349
Cdd:COG5000  197 --RLAAWgeLARRIAHEIKNPLTPIQLSAERLRrkladkLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARL----PE 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 350 MHCQLTEMSGLVDEVDKVHRLKMK-KGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIE-GSITFGLVKEEEWV 427
Cdd:COG5000  271 PQLEPVDLNELLREVLALYEPALKeKDIRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRREDGRV 350
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 794205150 428 KLYVTDTGCGISKEKLPLIFTRF----EKlndfvqGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG5000  351 RIEVSDNGPGIPEEVLERIFEPFfttkPK------GTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLP 416
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
261-635 1.30e-40

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 158.92  E-value: 1.30e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 261 RMRRS--QELL----EAKQRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLI 334
Cdd:PRK11466 417 KARTAelQELViehrQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTIL 496
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 335 NDILDLSRIESGKSEMhcqltemsGLVDE-------VDKVHRLkMKKGVKLNVIRPSEEI------WISTDRNRVTQVLF 401
Cdd:PRK11466 497 NDILDYSAIEAGGKNV--------SVSDEpfeprplLESTLQL-MSGRVKGRPIRLATDIaddlptALMGDPRRIRQVIT 567
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 402 NFLSNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVE 481
Cdd:PRK11466 568 NLLSNALRFTDEGSIVLRSRTDGEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSAT 647
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 482 SELGQGSTFILYLPNRQVQeVVVGERENAAGNMgveNRQKKILIAEDVESSYLQINAFLKKEYTILWVPNGEEAVKSFIR 561
Cdd:PRK11466 648 STPEVGSCFCLRLPLRVAT-APVPKTVNQAVRL---DGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQN 723
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 794205150 562 EKP-DLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:PRK11466 724 SEPfAAALVDFDLPDYDGITLARQLAQQYPSLVLIGFSAHVIDETLRQRTSSLFRGIIPKPVPREVLGQLLAHYL 798
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
264-499 6.00e-40

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


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 152.21  E-value: 6.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 264 RSQELLEAKQRAEEADRMK--SVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLS 341
Cdd:COG5808  221 KRKTLLERVIQEINTQKLEliGTFAASTAHEIRNPLTSIKGFIQLLQEKYPELEDQKYFDIIQEEIQRINQIVSEFLVLG 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 342 RIESGKSemhcQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFG 419
Cdd:COG5808  301 KPTAKKL----ELDDLNELIEEIlSIIDSEANLKNIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGGkLTIS 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 420 LVKEEEWVKLYVTDTGCGISKEKLPLIFTRF--EKLNdfvqGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNR 497
Cdd:COG5808  377 IENDDEKAVIEVIDNGEGIPEDIIDEIFEPFvtTKEG----GTGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTIRLPLK 452

                 ..
gi 794205150 498 QV 499
Cdd:COG5808  453 KE 454
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
398-495 5.31e-34

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: 125.30  E-value: 5.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNTIEGSITF-----GLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFV----QGTGLGLPICK 468
Cdd:cd16922    3 QILLNLLGNAIKFTEEGEVTLrvsleEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTtrkyGGTGLGLAISK 82
                         90       100
                 ....*....|....*....|....*..
gi 794205150 469 SIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16922   83 KLVELMGGDISVESEPGQGSTFTFTLP 109
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
516-635 6.55e-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: 125.73  E-value: 6.55e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 516 VENRQKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQ--EI 592
Cdd:COG0784    1 PPLGGKRILVVDDNPDNRELLRRLLERLgYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRlpDI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 794205150 593 PIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG0784   81 PIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLL 123
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
391-495 9.39e-33

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 121.60  E-value: 9.39e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150   391 TDRNRVTQVLFNFLSNAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF---EKLNDFVQGTGLGLPI 466
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFfrtDKRSRKIGGTGLGLSI 80
                           90       100
                   ....*....|....*....|....*....
gi 794205150   467 CKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:smart00387  81 VKKLVELHGGEISVESEPGGGTTFTITLP 109
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
47-495 1.50e-32

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: 131.39  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  47 FTDEYFHILGLKEAGIIFRDINDFYrfaHPEDVISYQTTFARMLESETKISQIVVRCvgRQGETIWLEDNfiAYKKNKEN 126
Cdd:COG5805   59 INPAMEKLLGYTSEEIIGKTIFDFL---EKEYHYRVKTRIERLQKGYDVVMIEQIYC--KDGELIYVEVK--LFPIYNQN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 127 GSDKIIAyTANITSRCEKEAQIRQLEERNRKIIEALPEFIFIFDDN-------FFITDVLMAPDTELLhpvevlkgadGR 199
Cdd:COG5805  132 GQAAILA-LRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDgrilfinESIERLFGAPREELI----------GK 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 200 SIYSSeVSDLFISSIHECLKSGKLKEIEYPVDVE----AGRH-FFQARIAPFEGNK-----VLALIHDIGDR------MR 263
Cdd:COG5805  201 NLLEL-LHPCDKEEFKERIESITEVWQEFIIEREiitkDGRIrYFEAVIVPLIDTDgsvkgILVILRDITEKkeaeelMA 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 264 RSQELLEAKQRAeeadrmksvflANMSHEIRTPLNAIVGFSEIIALTEDEKEkeEYLGIIQQNSNLLLQLINDILDLSRi 343
Cdd:COG5805  280 RSEKLSIAGQLA-----------AGIAHEIRNPLTSIKGFLQLLQPGIEDKE--EYFDIMLSELDRIESIISEFLALAK- 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 344 esgKSEMHCQLTEMSGLVDEVdkVHRLK---MKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFlsnaIKNTIE-----GS 415
Cdd:COG5805  346 ---PQAVNKEKENINELIQDV--VTLLEteaILHNIQIRLELLDEDPFIYCDENQIKQVFINL----IKNAIEampngGT 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 416 ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDfvQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:COG5805  417 ITIHTEEEDNSVIIRVIDEGIGIPEERLKKLGEPFFTTKE--KGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLP 494
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
523-631 2.88e-30

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: 114.87  E-value: 2.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA---ISQEIPIIAIT 598
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLgYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElegGGRRTPIIALT 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17546   81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
210-495 4.23e-30

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 125.47  E-value: 4.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 210 FISSIHECLKSGKL---KEIEYP-----VDVEAGrhffQARIAPFEGNKVLALI--HDIGDRMRrsqeLLEAKQRAEead 279
Cdd:PRK11360 317 FASPLLDTLEHGTEhvdLEISFPgrdrtIELSVS----TSLLHNTHGEMIGALVifSDLTERKR----LQRRVARQE--- 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 280 RMKSV--FLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRiesgKSEMHCQLTEM 357
Cdd:PRK11360 386 RLAALgeLVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSR----PRESQWQPVSL 461
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 358 SGLVDEVDKVHRLKMKKgVKLNVIRPSEE----IWIstDRNRVTQVLFNFLSN---AIKNTIEGSITFGLVKEEEwVKLY 430
Cdd:PRK11360 462 NALVEEVLQLFQTAGVQ-ARVDFETELDNelppIWA--DPELLKQVLLNILINavqAISARGKIRIRTWQYSDGQ-VAVS 537
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 794205150 431 VTDTGCGISKEKLPLIFTRFeklndFV---QGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:PRK11360 538 IEDNGCGIDPELLKKIFDPF-----FTtkaKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLP 600
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
261-495 3.49e-29

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 121.05  E-value: 3.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 261 RMRRSQELLEAKQRAEEadrmKSVFL----ANMSHEIRTPLNAIVGFSEIIA-LTEDEKEKEEYLGIIQQNSNLLLQLIN 335
Cdd:PRK10364 216 RYLRSRQLLQDEMKRKE----KLVALghlaAGVAHEIRNPLSSIKGLAKYFAeRAPAGGEAHQLAQVMAKEADRLNRVVS 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 336 DILDLSRiesgKSEMHCQLTEMSGLVDevdkvHRLKM------KKGVKLNvIRPSEEI-WISTDRNRVTQVLFNFLSNAI 408
Cdd:PRK10364 292 ELLELVK----PTHLALQAVDLNDLIN-----HSLQLvsqdanSREIQLR-FTANDTLpEIQADPDRLTQVLLNLYLNAI 361
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 409 KNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFekLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQG 487
Cdd:PRK10364 362 QAIGQhGVISVTASESGAGVKISVTDSGKGIAADQLEAIFTPY--FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKG 439

                 ....*...
gi 794205150 488 STFILYLP 495
Cdd:PRK10364 440 ATFTLWLP 447
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
273-495 4.12e-29

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: 120.96  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  273 QRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEiIALTEDeKEKEEYLGIIQqnSNL-----LLQLINDILDLSRIESGK 347
Cdd:TIGR01386 232 GRLEDAFQRLSQFSADLAHELRTPLTNLLGQTQ-VALSQP-RTGEEYREVLE--SNLeelerLSRMVSDMLFLARADNGQ 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  348 SemHCQLTEMSgLVDEVDKVHR----LKMKKGVKLNVirpSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVK 422
Cdd:TIGR01386 308 L--ALERVRLD-LAAELAKVAEyfepLAEERGVRIRV---EGEGLVRGDPQMFRRAISNLLSNALRHTPDGGtITVRIER 381
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 794205150  423 EEEWVKLYVTDTGCGISKEKLPLIFTRFEKLN----DFVQGTGLGLPICKSIVERLGGRIEVESeLGQGSTFILYLP 495
Cdd:TIGR01386 382 RSDEVRVSVSNPGPGIPPEHLSRLFDRFYRVDparsNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
260-635 6.90e-29

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 122.48  E-value: 6.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 260 DRMRRSQELLEAKQRAEEADRMKSV--FLANMSHEIRTPLNAIVGFSEI-IALTEDEKEKEEYLGIIQQNSNLLLQLIND 336
Cdd:PRK13837 426 ERRRLETERDALERRLEHARRLEAVgtLASGIAHNFNNILGAILGYAEMaLNKLARHSRAARYIDEIISAGARARLIIDQ 505
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 337 ILDLSRiesgKSEMHCQLTEMSGLVDEVDKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNA--------- 407
Cdd:PRK13837 506 ILAFGR----KGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAaqamdgagr 581
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 408 -------IKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFeklndFV---QGTGLGLPICKSIVERLGGR 477
Cdd:PRK13837 582 vdislsrAKLRAPKVLSHGVLPPGRYVLLRVSDTGAGIDEAVLPHIFEPF-----FTtraGGTGLGLATVHGIVSAHAGY 656
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 478 IEVESELGQGSTFILYLPnRQVQEVVVGERENAAGNMGVENRQKKILIAEDVES--SYLQINAFLKKEytilwvPNG--- 552
Cdd:PRK13837 657 IDVQSTVGRGTRFDVYLP-PSSKVPVAPQAFFGPGPLPRGRGETVLLVEPDDATleRYEEKLAALGYE------PVGfst 729
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 553 -EEAVkSFIREKP---DLILmdIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPeGERALEAGCNEVIAKPYPLEKLK 628
Cdd:PRK13837 730 lAAAI-AWISKGPerfDLVL--VDDRLLDEEQAAAALHAAAPTLPIILGGNSKTMA-LSPDLLASVAEILAKPISSRTLA 805

                 ....*..
gi 794205150 629 ETIETYL 635
Cdd:PRK13837 806 YALRTAL 812
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
391-495 1.15e-28

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: 110.15  E-value: 1.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  391 TDRNRVTQVLFNFLSNAIK-NTIEGSITFGlVKEEEWVKLYVTDTGCGISKEKLPLIFTRF-EKLNDFVQGTGLGLPICK 468
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKhAAKAGEITVT-LSEGGELTLTVEDNGIGIPPEDLPRIFEPFsTADKRGGGGTGLGLSIVR 79
                          90       100
                  ....*....|....*....|....*..
gi 794205150  469 SIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:pfam02518  80 KLVELLGGTITVESEPGGGTTVTLTLP 106
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
520-633 4.83e-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: 110.77  E-value: 4.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 520 QKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIA 596
Cdd:COG3706    1 PARILVVDDDPTNRKLLRRLLEAAgYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPrtADIPIIF 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 597 ITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:COG3706   81 LTALDDEEDRARALEAGADDYLTKPFDPEELLARVDL 117
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
522-632 3.57e-26

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: 103.39  E-value: 3.57e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAI--SQEIPIIAIT 598
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAgYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDpaTRDIPVIALT 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:cd17548   81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVA 114
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
520-635 6.97e-26

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: 105.42  E-value: 6.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 520 QKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:COG0745    1 MPRILVVEDDPDIRELLADALEREgYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRARPSDIPIIMLT 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG0745   81 ARDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALL 117
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
260-497 8.29e-26

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 111.09  E-value: 8.29e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 260 DRMRRSqelLEAKQRAEEadrmksvFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILD 339
Cdd:PRK11100 244 ESMRVK---LEGKAYVEQ-------YVQTLTHELKSPLAAIRGAAELLQEDPPPEDRARFTGNILTQSARLQQLIDRLLE 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 340 LSRIESGKSEMHCQLTEMSGLVDE-VDKVHRLKMKKGVKLNVIrpSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGS-IT 417
Cdd:PRK11100 314 LARLEQRQELEVLEPVALAALLEElVEAREAQAAAKGITLRLR--PDDARVLGDPFLLRQALGNLLDNAIDFSPEGGtIT 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 418 FGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL---NDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYL 494
Cdd:PRK11100 392 LSAEVDGEQVALSVEDQGPGIPDYALPRIFERFYSLprpANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTL 471

                 ...
gi 794205150 495 PNR 497
Cdd:PRK11100 472 PRH 474
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
523-632 1.59e-25

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: 101.46  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEgYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRRDPTTPVIILTAHG 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 794205150  602 FCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:pfam00072  81 DEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
273-497 2.24e-25

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 110.11  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 273 QRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEkekeeyLGIIQQNSNLLLQ--------LINDILDLSRIE 344
Cdd:NF040691 262 RQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSRDD------FDPATARSAELLHteldrfesLLSDLLEISRFD 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 345 SGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTiEGS---ITFGl 420
Cdd:NF040691 336 AGAAELDVEPVDLRPLVRRVvDALRQLAERAGVELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKpvvVTVA- 413
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 421 vKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPN 496
Cdd:NF040691 414 -QDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdparARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLTLPR 492

                 .
gi 794205150 497 R 497
Cdd:NF040691 493 V 493
PRK09303 PRK09303
histidine kinase;
262-495 6.31e-25

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 106.96  E-value: 6.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 262 MRRSQELLEAKQRAEE-ADRMKSV--FLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQnsnLLLQ------ 332
Cdd:PRK09303 128 LQLSDELFVLRQENETlLEQLKFKdrVLAMLAHDLRTPLTAASLALETLELGQIDEDTELKPALIEQ---LQDQarrqle 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 333 ----LINDILDLSRIESGKSEMHCQLTEMSGLVDEV-DKVHRLKMKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNA 407
Cdd:PRK09303 205 eierLITDLLEVGRTRWEALRFNPQKLDLGSLCQEViLELEKRWLAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNA 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 408 IKNTIE-GSITF-GLVKEEEWVKLYVTDTGCGISKEKLPLIFT-RFEKLNDFVQ-GTGLGLPICKSIVERLGGRIEVESE 483
Cdd:PRK09303 285 IKYTPEgGTITLsMLHRTTQKVQVSICDTGPGIPEEEQERIFEdRVRLPRDEGTeGYGIGLSVCRRIVRVHYGQIWVDSE 364
                        250
                 ....*....|..
gi 794205150 484 LGQGSTFILYLP 495
Cdd:PRK09303 365 PGQGSCFHFTLP 376
PRK10490 PRK10490
sensor protein KdpD; Provisional
267-502 1.20e-24

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 109.36  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 267 ELLEAKQRAEEA------DRMKSVFLANMSHEIRTPLNAIVGFSEIIAL---TEDEKEKEEYLGIIQQNSNLLlQLINDI 337
Cdd:PRK10490 643 ERLTLTASEEQArlaserEQLRNALLAALSHDLRTPLTVLFGQAEILTLdlaSEGSPHARQASEIRQQVLNTT-RLVNNL 721
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 338 LDLSRIESGKSEMHCQ---LTEMSGlvdevDKVHRLK-MKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIE 413
Cdd:PRK10490 722 LDMARIQSGGFNLRKEwltLEEVVG-----SALQMLEpGLSGHPINLSLPEPLTLIHVDGPLFERVLINLLENAVKYAGA 796
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 414 GS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLN--DFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTF 490
Cdd:PRK10490 797 QAeIGIDAHVEGERLQLDVWDNGPGIPPGQEQLIFDKFARGNkeSAIPGVGLGLAICRAIVEVHGGTIWAENRPEGGACF 876
                        250
                 ....*....|..
gi 794205150 491 ILYLPNRQVQEV 502
Cdd:PRK10490 877 RVTLPLETPPEL 888
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
519-635 2.73e-24

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: 101.40  E-value: 2.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 519 RQKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPII 595
Cdd:COG3437    5 QAPTVLIVDDDPENLELLRQLLRTLgYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPstRDIPVI 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 794205150 596 AITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG3437   85 FLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
519-635 2.30e-23

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: 103.12  E-value: 2.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 519 RQKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAgYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRALDPDLPVILL 80
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG2204   81 TGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERAL 118
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
521-635 3.03e-23

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 95.25  E-value: 3.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:COG5803    3 KKILIVDDQAGIRMLLKEVLKKEgYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPDIPVIMMTA 82
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG5803   83 YGELDMVEEAKELGAKGYFTKPFDIDELREAVNKLL 118
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
524-621 6.77e-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: 90.36  E-value: 6.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 524 LIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAF 602
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREgYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAKAD 80
                         90
                 ....*....|....*....
gi 794205150 603 CPEGERALEAGCNEVIAKP 621
Cdd:cd00156   81 EEDAVRALELGADDYLVKP 99
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
522-621 9.63e-22

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


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 90.22  E-value: 9.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE---YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEagfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIRELDPDTKIIILS 80
                         90       100
                 ....*....|....*....|...
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKP 621
Cdd:COG4753   81 GYSDFEYAQEAIKLGADDYLLKP 103
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
273-497 7.79e-21

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 95.99  E-value: 7.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 273 QRAEEADRMKSVFLANMSHEIRTPLNAIVGFSEIiALTED--EKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEM 350
Cdd:PRK09835 253 ERIEDVFTRQSNFSADIAHEIRTPITNLITQTEI-ALSQSrsQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIP 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 351 HCQlteMSGLVDEVDKV----HRLKMKKGVKLNVIrpSEEIWISTDRNRVTQVLFNFLSNAIKNTIEG-SITFGLVKEEE 425
Cdd:PRK09835 332 EKK---MLDLADEVGKVfdffEAWAEERGVELRFV--GDPCQVAGDPLMLRRAISNLLSNALRYTPAGeAITVRCQEVDH 406
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 794205150 426 WVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQ----GTGLGLPICKSIVERLGGRIEVESELgQGSTFILYLPNR 497
Cdd:PRK09835 407 QVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQrkgeGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVISLPRL 481
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
519-635 8.89e-21

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 88.87  E-value: 8.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 519 RQKKILIAEDvESSYLQINA-FLKKEY---TILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPI 594
Cdd:COG4565    2 KMIRVLIVED-DPMVAELLRrYLERLPgfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRARGPDVDV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 794205150 595 IAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:COG4565   81 IVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
239-495 9.48e-21

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 95.66  E-value: 9.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 239 FQARIAPFEGNKVLALIHDigdrMRRSQELLEAKQRaeeadrMKSVFLANMSHEIRTPLNAIVGFSEIIaltED--EKEK 316
Cdd:NF012163 207 YTTRVTPTSNDELGKLAQD----FNQLASTLEKNEQ------MRRDFMADISHELRTPLAVLRAELEAI---QDgiRKFT 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 317 EEYLGIIQQNSNLLLQLINDILDLSRIESGksEMHCQLTEMS--GLVDEVDKVHRLKM-KKGVKLNVIRPsEEIWISTDR 393
Cdd:NF012163 274 PESLDSLQAEVGTLTKLVDDLHDLSMSDEG--ALAYQKASVDlvPLLEVEGGAFRERFaSAGLELEVSLP-DSSLVFGDR 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 394 NRVTQVLFNFLSNAIKNT-IEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPICK 468
Cdd:NF012163 351 DRLMQLFNNLLENSLRYTdSGGSLHISASQRPKEVTLTVADSAPGVSDEQLARLFERFYRVevsrNRASGGSGLGLAISL 430
                        250       260
                 ....*....|....*....|....*...
gi 794205150 469 SIVERLGGRIEVE-SELGqGSTFILYLP 495
Cdd:NF012163 431 NIVQAHGGTLHAAhSPLG-GLRIVVTLP 457
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
281-346 3.97e-20

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 84.19  E-value: 3.97e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 794205150  281 MKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESG 346
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
281-346 7.86e-20

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 83.38  E-value: 7.86e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 794205150   281 MKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESG 346
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-495 9.23e-20

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: 84.69  E-value: 9.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNTIEGS---ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLN--DFVQGTGLGLPICKSIVE 472
Cdd:cd16921    3 QVLTNLLGNAIKFRRPRRpprIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHsrEEYEGTGVGLAIVRKIIE 82
                         90       100
                 ....*....|....*....|...
gi 794205150 473 RLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16921   83 RHGGRIWLESEPGEGTTFYFTLP 105
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
235-497 1.45e-19

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 91.61  E-value: 1.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 235 GRHFfQARIAPFEGNKVLALIHDIgDRMRRsqelLEAKQRAeeadrmksvFLANMSHEIRTPLNAIVGFSEiiaLTEDE- 313
Cdd:PRK11006 172 GRHL-EIRVMPYTEGQLLMVARDV-TQMHQ----LEGARRN---------FFANVSHELRTPLTVLQGYLE---MMQDQp 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 314 ---KEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSemhcqlTEMSGLVD-----EV---------DKVHRLKMKKGV 376
Cdd:PRK11006 234 legALREKALHTMREQTQRMEGLVKQLLTLSKIEAAPT------IDLNEKVDvpmmlRVlereaqtlsQGKHTITFEVDN 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 377 KLNVIRPSEEIwistdRNRVTqvlfNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLND 455
Cdd:PRK11006 308 SLKVFGNEDQL-----RSAIS----NLVYNAVNHTPEGThITVRWQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDK 378
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 794205150 456 F----VQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLPNR 497
Cdd:PRK11006 379 ArsrqTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPER 424
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
393-495 1.90e-19

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: 83.63  E-value: 1.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 393 RNRVTQVLFNFLSNAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIV 471
Cdd:cd16943    1 PSQLNQVLLNLLVNAAQAMEGrGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGEGTGLGLSLSYRII 80
                         90       100
                 ....*....|....*....|....
gi 794205150 472 ERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16943   81 QKHGGTIRVASVPGGGTRFTIILP 104
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
251-495 2.71e-19

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 90.29  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 251 VLALIHDIGDRMRRSQELLEAKQRAEEadrmksvfLANMSHEIRTPLNAIVGFSEIialtedeKEKEEylgiiqqnsnlL 330
Cdd:COG3290  166 AVATFRDRTELERLEEELEGVKELAEA--------LRAQRHDFRNHLHTISGLLQL-------GEYDE-----------A 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 331 LQLINDILDLSRIESGKSEMHCQLTEMSGLVdeVDKVHRLKmKKGVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAI-- 408
Cdd:COG3290  220 LEYIDEISEELQELIDSLLSRIGNPVLAALL--LGKAARAR-ERGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIea 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 409 ---KNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTR--FEKLNDfvqGTGLGLPICKSIVERLGGRIEVESE 483
Cdd:COG3290  297 vekLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFERgfSTKLGE---GRGLGLALVKQIVEKYGGTIEVESE 373
                        250
                 ....*....|..
gi 794205150 484 LGQGSTFILYLP 495
Cdd:COG3290  374 EGEGTVFTVRLP 385
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
522-622 3.12e-19

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: 82.93  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAI--SQEIPIIAIT 598
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEgYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDpeTRHIPVIMIT 80
                         90       100
                 ....*....|....*....|....*..
gi 794205150 599 AYAfcpEGE---RALEAGCNEVIAKPY 622
Cdd:cd17538   81 ALD---DREdriRGLEAGADDFLSKPI 104
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
521-631 5.50e-19

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 82.65  E-value: 5.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESsylqINAFLKKE-----YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPII 595
Cdd:cd17554    1 KKILVVDDEEN----IRELYKEEledegYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVI 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 794205150 596 AITAYAFCPEGERALEAGcnEVIAKPYPLEKLKETI 631
Cdd:cd17554   77 ICTAYSEYKSDFSSWAAD--AYVVKSSDLTELKETI 110
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
521-635 1.55e-18

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: 81.68  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTIL-WVPNGEEAVKSFIREKPDLILMDIRMP-VMNGIQATAKIRAISQeIPIIAI 597
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLgYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD-IPVIFL 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 794205150 598 TAYA----FcpegERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17534   80 TAYSdeetL----ERAKETNPYGYLVKPFNERELKAAIELAL 117
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
523-631 2.31e-18

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: 80.96  E-value: 2.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIAITA 599
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEgAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPwlANTPAIALTG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17580   81 YGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
551-633 3.62e-18

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: 80.63  E-value: 3.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKET 630
Cdd:cd17535   32 DGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEA 111

                 ...
gi 794205150 631 IET 633
Cdd:cd17535  112 IRA 114
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
524-621 3.88e-18

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: 79.76  E-value: 3.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 524 LIAEDvESSYLQ-INAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYa 601
Cdd:cd17574    1 LVVED-DEEIAElLSDYLEKEgYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAK- 78
                         90       100
                 ....*....|....*....|....
gi 794205150 602 fcpEGE----RALEAGCNEVIAKP 621
Cdd:cd17574   79 ---DEEedkvLGLELGADDYITKP 99
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
522-628 4.19e-18

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 87.21  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAY 600
Cdd:PRK11361   6 RILIVDDEDNVRRMLSTAFALQgFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETRTPVILMTAY 85
                         90       100
                 ....*....|....*....|....*...
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYPLEKLK 628
Cdd:PRK11361  86 AEVETAVEALRCGAFDYVIKPFDLDELN 113
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
522-621 2.89e-17

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: 78.20  E-value: 2.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDveSSYLQinAFLKK------EYTILWV-PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPI 594
Cdd:cd17541    2 RVLIVDD--SAVMR--KLLSRilesdpDIEVVGTaRDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAER-PTPV 76
                         90       100       110
                 ....*....|....*....|....*....|.
gi 794205150 595 IAITAYAfcPEGE----RALEAGCNEVIAKP 621
Cdd:cd17541   77 VMVSSLT--EEGAeitlEALELGAVDFIAKP 105
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
391-495 3.32e-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: 77.71  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 391 TDRNRVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF---EKLNDFVQGTGLGLPI 466
Cdd:cd16948    1 TDAKWLSFIIGQIVSNALKYSKQGGkIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGftgENGRNFQESTGMGLYL 80
                         90       100
                 ....*....|....*....|....*....
gi 794205150 467 CKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16948   81 VKKLCDKLGHKIDVESEVGEGTTFTITFP 109
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
276-495 4.94e-17

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 84.30  E-value: 4.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 276 EEADRMKSVFLANMSHEIRTPLNAIVGfsEIIALtED--EKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKsemhcq 353
Cdd:PRK10549 234 EKNEQMRRDFMADISHELRTPLAVLRG--ELEAI-QDgvRKFTPESVASLQAEVGTLTKLVDDLHQLSLSDEGA------ 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 354 LTEMSGLVDEVDKV--------HRLKmKKGVKLNVIRPsEEIWISTDRNRVTQVLFNFLSNAIKNTIE-GSITFGLVKEE 424
Cdd:PRK10549 305 LAYRKTPVDLVPLLevaggafrERFA-SRGLTLQLSLP-DSATVFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRD 382
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 794205150 425 EWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPICKSIVERLGGRIEVE-SELGqGSTFILYLP 495
Cdd:PRK10549 383 KTLRLTFADSAPGVSDEQLQKLFERFYRTegsrNRASGGSGLGLAICLNIVEAHNGRIIAAhSPFG-GVSITVELP 457
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
279-342 8.43e-17

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: 74.94  E-value: 8.43e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 794205150 279 DRMKSVFLANMSHEIRTPLNAIVGFSEIIALTEDEKEK-EEYLGIIQQNSNLLLQLINDILDLSR 342
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEqREYLERIREEAERLLRLINDLLDLSR 65
PRK13557 PRK13557
histidine kinase; Provisional
413-622 1.26e-16

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 83.18  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 413 EGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFIL 492
Cdd:PRK13557 311 EDLAMYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRL 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 493 YLPNRQVQEVVVGERENAAGNMGVENRqkkILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIRE-KPDLILMD 570
Cdd:PRK13557 391 YFPASDQAENPEQEPKARAIDRGGTET---ILIVDDRPDVAELARMILEDFgYRTLVASNGREALEILDSHpEVDLLFTD 467
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 794205150 571 IRMP-VMNGIQATAKIRAISQEIPIIAITAYAfcpegERALE---AGCNE--VIAKPY 622
Cdd:PRK13557 468 LIMPgGMNGVMLAREARRRQPKIKVLLTTGYA-----EASIErtdAGGSEfdILNKPY 520
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
551-632 1.42e-16

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 76.22  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA-FcpegE---RALEAGCNEVIAKPYPLEK 626
Cdd:cd17536   33 NGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRELYPDIKIIILSGYDdF----EyaqKAIRLGVVDYLLKPVDEEE 108

                 ....*.
gi 794205150 627 LKETIE 632
Cdd:cd17536  109 LEEALE 114
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
392-495 1.46e-16

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: 75.58  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 392 DRNRVTQVLFNFLSNAIKNTIEG-SITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL----NDFVQGTGLGLPI 466
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGgKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVessrNRASGGSGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 467 CKSIVERLGGRIEVE-SELGqGSTFILYLP 495
Cdd:cd16946   81 CHNIALAHGGTISAEhSPLG-GLRLVLTLP 109
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
521-632 3.62e-16

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: 75.01  E-value: 3.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE--YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAgyEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDPNAKVIMCS 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:cd17542   81 AMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVE 114
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-498 1.25e-15

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: 73.01  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 402 NFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDF----VQGTGLGLPICKSIVERLGG 476
Cdd:cd16952    7 NLVSNAVKYTPPSDtITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRVDIErcrnTGGTGLGLAIVKHVMSRHDA 86
                         90       100
                 ....*....|....*....|..
gi 794205150 477 RIEVESELGQGSTFILYLPNRQ 498
Cdd:cd16952   87 RLLIASELGKGSRFTCLFPSSR 108
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
521-633 5.82e-15

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: 71.29  E-value: 5.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILW-VPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRaiSQEI-PIIAI 597
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAgYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIIT--SENIaPIVLL 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:cd19932   79 TAYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEM 114
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
396-495 6.33e-15

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: 70.89  E-value: 6.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 396 VTQVLFNFLSNAIKNTIEG-------SITFGlVKEEEWVKLYVTDTGCGISKEKLPLIFTRFekLNDFVQGTGLGLPICK 468
Cdd:cd16920    1 IQQVLINLVRNGIEAMSEGgcerrelTIRTS-PADDRAVTISVKDTGPGIAEEVAGQLFDPF--YTTKSEGLGMGLSICR 77
                         90       100
                 ....*....|....*....|....*..
gi 794205150 469 SIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16920   78 SIIEAHGGRLSVESPAGGGATFQFTLP 104
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
522-632 7.80e-15

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 74.47  E-value: 7.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKK--EYTIL-WVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKypDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 599 AYAfcpegERALEAGCNEVIA---KPYPLEKLKETIE 632
Cdd:COG3279   83 AYD-----EYALEAFEVNAVDyllKPIDEERLAKALE 114
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
355-485 1.08e-14

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: 71.12  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 355 TEMSGLVDEVDKVHRlkmKKGVKLNViRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIEgSITFGLVKEEEWVKLYVTDT 434
Cdd:cd16954    1 PLLDSLCSALNKVYQ---RKGVSISL-DISPELRFPGERNDLMELLGNLLDNACKWCLE-FVEVTARQTDGGLHLIVDDD 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 794205150 435 GCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVE-SELG 485
Cdd:cd16954   76 GPGVPESQRSKIFQRGQRLDEQRPGQGLGLAIAKEIVEQYGGELSLSdSPLG 127
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
523-622 1.68e-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: 69.46  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA--ISQEIPIIAITA 599
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAgYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKAdpATRHIPVIFLTA 80
                         90       100
                 ....*....|....*....|...
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPY 622
Cdd:cd19920   81 LTDTEDKVKGFELGAVDYITKPF 103
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
396-494 1.74e-14

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: 69.41  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 396 VTQVLFNFLSNA---IKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVE 472
Cdd:cd16976    1 IQQVLMNLLQNAldaMGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGKGTGLGLSISYGIVE 80
                         90       100
                 ....*....|....*....|..
gi 794205150 473 RLGGRIEVESELGQGSTFILYL 494
Cdd:cd16976   81 EHGGRLSVANEEGAGARFTFDL 102
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
522-622 2.46e-14

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 69.78  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESS------------YLQINAFLkkeytilwvpNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS 589
Cdd:cd17551    2 RILIVDDNPTNlllleallrsagYLEVVSFT----------DPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALP 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 794205150 590 --QEIPIIAITAYafcPEGE---RALEAGCNEVIAKPY 622
Cdd:cd17551   72 glEDVPIVMITAD---TDREvrlRALEAGATDFLTKPF 106
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
522-631 1.16e-13

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 67.49  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAITAY 600
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAES-GVPIVMLTAK 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYpleKLKETI 631
Cdd:cd17626   81 SDTVDVVLGLESGADDYVAKPF---KPKELV 108
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
384-487 1.22e-13

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


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 67.43  E-value: 1.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 384 SEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLN-DFVQGTGL 462
Cdd:cd16940    2 AADIQVQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKLSADDGAVIRVEDNGPGIDEEELEALFERFYRSDgQNYGGSGL 81
                         90       100
                 ....*....|....*....|....*
gi 794205150 463 GLPICKSIVERLGGRIEVESELGQG 487
Cdd:cd16940   82 GLSIVKRIVELHGGQIFLGNAQGGG 106
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
523-627 1.32e-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: 67.41  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESsylqINAFLKKE-----YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:cd17627    1 ILVVDDDRA----VRESLRRSlrfegYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGNDLPILVL 76
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17627   77 TARDSVSDRVAGLDAGADDYLVKPFALEEL 106
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
413-495 1.96e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 66.54  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 413 EGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIF-----TRFEKlndfvqGTGLGLPICKSIVERLGGRIEVESELGQG 487
Cdd:cd16915   23 NKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFergvsTKGQG------ERGIGLALVRQSVERLGGSITVESEPGGG 96

                 ....*...
gi 794205150 488 STFILYLP 495
Cdd:cd16915   97 TTFSIRIP 104
orf27 CHL00148
Ycf27; Reviewed
517-635 3.67e-13

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 69.36  E-value: 3.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 517 ENRQKKILIAEDvESSYLQInafLKKE-----YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqE 591
Cdd:CHL00148   3 ENSKEKILVVDD-EAYIRKI---LETRlsiigYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKES-D 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 794205150 592 IPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:CHL00148  78 VPIIMLTALGDVSDRITGLELGADDYVVKPFSPKELEARIRSVL 121
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
521-635 4.14e-13

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: 66.04  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEgYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMKVIDENIRVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17553   81 YGELDMIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
258-495 5.56e-13

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 72.03  E-value: 5.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 258 IGDRMRRSQELLEAKQRAEEADRMKSV--FLANMSHEIRTPLNAI--VGFSEIIALtedEKEKEEYLGIIQQNSNLLLQL 333
Cdd:COG4192  407 IEERKRIEKNLRQTQDELIQAAKMAVVgqTMTSLAHELNQPLNAMsmYLFSAKKAL---EQENYAQLPTSLDKIEGLIER 483
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 334 INDILDLSRIESGKSEMHCQLTEMSGLVDEVDKVHRLKMKKgvKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIKNTIE 413
Cdd:COG4192  484 MDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKP--QQITLHIPDDLMVQGDQVLLEQVLVNLLVNALDAVAT 561
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 414 GS-ITFGLVKEEEWVKLYVTDTGCGIS-KEKLPLIFTRFEKLndfvqGTGLGLPICKSIVERLGGRIEVESELGQGSTFI 491
Cdd:COG4192  562 QPqISVDLLSNAENLRVAISDNGNGWPlVDKLFTPFTTTKEV-----GLGLGLSICRSIMQQFGGDLYLASTLERGAMVI 636

                 ....
gi 794205150 492 LYLP 495
Cdd:COG4192  637 LEFN 640
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
519-633 6.79e-13

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


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 67.67  E-value: 6.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 519 RQKKILIAEDVESSYLQINAFLKKE-YTIL-WVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAiSQEIPIIA 596
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAgYEVVaEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISE-ERPAPVIL 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 597 ITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:COG3707   81 LTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALEL 117
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
522-633 1.42e-12

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: 64.74  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKK---EYTILWVPNGEEAVKsFIR--------EKPDLILMDIRMPVMNGIQATAKIRAISQ 590
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEagvPNELHVVRDGEEALD-FLRgegeyadaPRPDLILLDLNMPRMDGFEVLREIKADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 794205150 591 --EIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:cd17557   80 lrRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
426-495 1.61e-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: 1.61e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 426 WVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16919   47 YVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVGKGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
521-625 2.14e-12

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 64.11  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE--YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIA 596
Cdd:cd17552    2 KRILVIDDEEDIREVVQACLEKLagWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPetQSIPVIL 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 597 ITAYAFCPEGERALEAGCNEVIAKPY-PLE 625
Cdd:cd17552   82 LTAKAQPSDRQRFASLGVAGVIAKPFdPLT 111
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
521-621 2.41e-12

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: 63.76  E-value: 2.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSgFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG 80
                         90       100
                 ....*....|....*....|..
gi 794205150 600 YAFCPEGERALEAGCNEVIAKP 621
Cdd:cd17555   81 AGVMSDAVEALRLGAWDYLTKP 102
PRK10693 PRK10693
two-component system response regulator RssB;
551-635 3.86e-12

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 67.32  E-value: 3.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYP-LEKLKE 629
Cdd:PRK10693   5 NGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKPVKdLNRLRE 84

                 ....*.
gi 794205150 630 TIETYL 635
Cdd:PRK10693  85 MVFACL 90
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
383-494 4.28e-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: 63.69  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 383 PSEEIWISTDRNRVTQVLFNFLSNAIKNTIEGSIT-FGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF----EKLNDFV 457
Cdd:cd16947    8 PDRPIYANANTEALQRILKNLISNAIKYGSDGKFLgMTLREDEKHVYIDIWDKGKGISETEKDHVFERLytleDSRNSAK 87
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 458 QGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYL 494
Cdd:cd16947   88 QGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
523-633 5.38e-12

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: 63.06  E-value: 5.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE---YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd19930    1 VLIAEDQEMVRGALAALLELEddlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREELPDTKVLIVTT 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLKDRPIEELADAIRT 114
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
392-495 8.24e-12

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: 62.12  E-value: 8.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 392 DRNRVTQVLFNFLSNAIKNTIEGsitfGLVK------EEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDFVQ----GTG 461
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDG----GRIRcilekfRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTrahgGTG 76
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 462 LGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16925   77 LGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
391-495 1.05e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 67.63  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 391 TDRNRVTQVLFNFLSNAIKNTIE-------GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTR-FEKLNDfvqGTGL 462
Cdd:PRK11086 425 SGDEDQVHELITILGNLIENALEavggeegGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKgYSTKGS---NRGV 501
                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205150 463 GLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:PRK11086 502 GLYLVKQSVENLGGSIAVESEPGVGTQFFVQIP 534
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
523-622 1.36e-11

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: 61.96  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIAITA 599
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQgYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTT 80
                         90       100
                 ....*....|....*....|...
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPY 622
Cdd:cd17598   81 LSDPRDVIRGLECGADNFITKPY 103
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
252-508 1.64e-11

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 67.65  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 252 LALIHD------IGDRMRRSQELLEAKQRAEEAdrmksvFLANMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQ 325
Cdd:PRK10618 420 LFLLRDqdrevlVNKKLQQAQREYEKNQQARKA------FLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAE 493
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 326 NSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV--DKVHRLKmKKGVKL--NVIRPSEEIWIStDRNRVTQVLF 401
Cdd:PRK10618 494 QSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVlpEVLPAIK-RKGLQLliHNHLKAEQLRIG-DRDALRKILL 571
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 402 NFLSNAIKNTIEGSITFGLVKEE---EWVKLYVTDTGCGISKEKLPLIftRFEKLND-----FVQGTGLGLPICKSIVER 473
Cdd:PRK10618 572 LLLNYAITTTAYGKITLEVDQDEsspDRLTIRILDTGAGVSIKELDNL--HFPFLNQtqgdrYGKASGLTFFLCNQLCRK 649
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 794205150 474 LGGRIEVESELGQGSTFILYLPNRQVQEVVVGERE 508
Cdd:PRK10618 650 LGGHLTIKSREGLGTRYSIHLKMLAADPEVEEEEE 684
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
527-632 2.08e-11

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: 61.74  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 527 EDVESSYLQinAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEG 606
Cdd:cd17549    8 ADVREALQQ--TLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIRELDPDLPVILITGHGDVPMA 85
                         90       100
                 ....*....|....*....|....*.
gi 794205150 607 ERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:cd17549   86 VEAMRAGAYDFLEKPFDPERLLDVVR 111
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
523-635 2.09e-11

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 61.14  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKK-EYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAITAYA 601
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKwGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQISN-VPIIFISSRD 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd18159   80 DNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
PRK10604 PRK10604
sensor protein RstB; Provisional
282-495 2.60e-11

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 66.17  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 282 KSVFLANMSHEIRTPLnaiVGFSEIIALTEDEKEKEeylgiiQQ--NSNL--LLQLINDILDLSRIESGKSEMHCQLTEM 357
Cdd:PRK10604 212 KKQLIDGIAHELRTPL---VRLRYRLEMSDNLSAAE------SQalNRDIgqLEALIEELLTYARLDRPQNELHLSEPDL 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 358 SG-LVDEVDKVHRLKMKKGVKLNviRPSEEIWISTDRNRVTQVLFNFLSNAIKNTiEGSITFGLVKEEEWVKLYVTDTGC 436
Cdd:PRK10604 283 PAwLSTHLADIQAVTPEKTVRLD--TPHQGDYGALDMRLMERVLDNLLNNALRYA-HSRVRVSLLLDGNQACLIVEDDGP 359
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 794205150 437 GISKEKLPLIFTRFEKL----NDFVQGTGLGLPICKSIVERLGGRIEVE-SELGqGSTFILYLP 495
Cdd:PRK10604 360 GIPPEERERVFEPFVRLdpsrDRATGGCGLGLAIVHSIALAMGGSVNCDeSELG-GARFSFSWP 422
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
523-621 3.87e-11

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: 59.87  E-value: 3.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVEssylQINAFLKKE-----YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAI 597
Cdd:cd17620    1 ILVIEDEP----QIRRFLRTAleahgYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREWSA-VPVIVL 75
                         90       100
                 ....*....|....*....|....*.
gi 794205150 598 TAYafCPEGE--RALEAGCNEVIAKP 621
Cdd:cd17620   76 SAR--DEESDkiAALDAGADDYLTKP 99
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
523-635 5.17e-11

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: 60.13  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVE--SSYLQINafLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAITA 599
Cdd:cd17614    1 ILVVDDEKpiSDILKFN--LTKEgYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKTS-NVPIIMLTA 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17614   78 KDSEVDKVLGLELGADDYVTKPFSNRELLARVKANL 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
521-632 5.88e-11

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 59.98  E-value: 5.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVES-SYLQINAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd19919    1 KTVWIVDDDSSiRWVLERALAGAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRHPDLPVIIMTA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:cd19919   81 HSDLDSAVSAYQGGAFEYLPKPFDIDEAVALVE 113
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
543-621 6.58e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 64.13  E-value: 6.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 543 EYTILWV-PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAITAyafCPEGE-----RALEAGCNE 616
Cdd:PRK12555  25 DHEVVWVaTDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAER-PCPILIVTS---LTERNasrvfEAMGAGALD 100

                 ....*
gi 794205150 617 VIAKP 621
Cdd:PRK12555 101 AVDTP 105
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
523-621 7.00e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 59.31  E-value: 7.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLK-KEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIAITA 599
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEdQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFLTA 80
                         90       100
                 ....*....|....*....|..
gi 794205150 600 YAFCPEGERALEAGCNEVIAKP 621
Cdd:cd19927   81 KGMTSDRIKGYNAGCDGYLSKP 102
glnL PRK11073
nitrogen regulation protein NR(II);
188-497 7.05e-11

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 64.33  E-value: 7.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 188 HPVEVLKGADGRSIYSSEVSDLF------ISSIHECLKSGK-LKEIEYPVDVEAGRHFFQARIAPFEGNKVLALIHDIGD 260
Cdd:PRK11073  34 PAAQQLLAQSSRKLFGTPLPELLsyfslnIELMRESLQAGQgFTDNEVTLVIDGRSHILSLTAQRLPEGMILLEMAPMDN 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 261 RMRRSQELLEAKQRAEEADRMKSvflanMSHEIRTPLNAIVGFSEIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDL 340
Cdd:PRK11073 114 QRRLSQEQLQHAQQVAARDLVRG-----LAHEIKNPLGGLRGAAQLLSKALPDPALTEYTKVIIEQADRLRNLVDRLLGP 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 341 SRIESGKSEMHCQLTEmsglvdevdKVHRL-KMKKGVKLNVIR---PS--EeiwISTDRNRVTQVLFNFLSNAIKNTIE- 413
Cdd:PRK11073 189 QRPGTHVTESIHKVAE---------RVVQLvSLELPDNVRLIRdydPSlpE---LAHDPDQIEQVLLNIVRNALQALGPe 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 414 -GSIT------FGLVKEEEWVKLY----VTDTGCGISKEKLPLIFtrFEKLNDFVQGTGLGLPICKSIVERLGGRIEVES 482
Cdd:PRK11073 257 gGTITlrtrtaFQLTLHGERYRLAaridIEDNGPGIPPHLQDTLF--YPMVSGREGGTGLGLSIARNLIDQHSGKIEFTS 334
                        330
                 ....*....|....*
gi 794205150 483 ELGQgSTFILYLPNR 497
Cdd:PRK11073 335 WPGH-TEFSVYLPIR 348
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
522-622 7.85e-11

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: 59.05  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKP-DLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAgYAVTEAESGAEALEKLQQGKDiDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
                         90       100
                 ....*....|....*....|....
gi 794205150 600 YAfCPEGERALEA-GCNEVIAKPY 622
Cdd:cd18160   81 GA-AAAPELLSDAvGDNATLKKPF 103
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
522-622 8.36e-11

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: 59.84  E-value: 8.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKsFIREKPD--LILMDIRMPVMNGIQATAKIRAI--SQEIPIIA 596
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHnFQVLEAANGQEALE-VLEQHPDikLVITDYNMPEMDGFELVREIRKKysRDQLAIIG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 794205150 597 ITAYafcpeGERALEA-----GCNEVIAKPY 622
Cdd:cd17544   81 ISAS-----GDNALSArfikaGANDFLTKPF 106
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
523-635 1.06e-10

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 64.28  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKK-EYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:PRK10365   8 ILVVDDDISHCTILQALLRGwGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPAIPVLIMTAYS 87
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:PRK10365  88 SVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
550-621 1.45e-10

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 63.25  E-value: 1.45e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 794205150 550 PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPII---AITAyafcpEGE----RALEAGCNEVIAKP 621
Cdd:PRK00742  36 PDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKIMRLR-PTPVVmvsSLTE-----RGAeitlRALELGAVDFVTKP 108
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
522-623 1.55e-10

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 58.93  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKK-EYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEiPIIAITAY 600
Cdd:cd17622    2 RILLVEDDPKLARLIADFLEShGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQG-PILLLTAL 80
                         90       100
                 ....*....|....*....|...
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYP 623
Cdd:cd17622   81 DSDIDHILGLELGADDYVVKPVE 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
551-632 1.55e-10

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 58.89  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQ--EIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLK 628
Cdd:cd19923   33 DGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGAlsHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLK 112

                 ....
gi 794205150 629 ETIE 632
Cdd:cd19923  113 EKLE 116
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
523-632 2.04e-10

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: 58.28  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEgYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHG 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETIE 632
Cdd:cd17550   81 TIETAVKATKLGAYDFIEKPLSLDRLLLTIE 111
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
524-635 3.13e-10

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 58.00  E-value: 3.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 524 LIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAF 602
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEgYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIETPVLLLTALDA 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 794205150 603 CPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17625   81 VEDRVKGLDLGADDYLPKPFSLAELLARIRALL 113
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
551-632 5.31e-10

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: 57.16  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAfcpegERALEAgcNEVIA-----KPYPLE 625
Cdd:cd17532   32 NGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKLSKLAKPPLIVFVTAYD-----EYAVEA--FELNAvdyllKPFSEE 104

                 ....*..
gi 794205150 626 KLKETIE 632
Cdd:cd17532  105 RLAEALA 111
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
521-634 6.55e-10

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: 56.78  E-value: 6.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKEY--TILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPADWdvEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLETKVIVVS 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 599 AyAFCPEG-ERALEAGCNEVIAKPYPLEKLKETIETY 634
Cdd:cd17593   81 G-DVQPEAkERVLELGALAFLKKPFDPEKLAQLLEEL 116
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
540-622 6.79e-10

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: 56.90  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 540 LKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAI--SQEIPIIAITAyafcpEGERA-----LE 611
Cdd:cd19937   17 LEKEgYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDpkTSSIPIIMLTA-----KGEEFdkvlgLE 91
                         90
                 ....*....|.
gi 794205150 612 AGCNEVIAKPY 622
Cdd:cd19937   92 LGADDYITKPF 102
pleD PRK09581
response regulator PleD; Reviewed
522-621 9.43e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 61.07  E-value: 9.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKEY-TILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA--ISQEIPIIAIT 598
Cdd:PRK09581   4 RILVVDDIPANVKLLEAKLLAEYyTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSdpATTHIPVVMVT 83
                         90       100
                 ....*....|....*....|...
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKP 621
Cdd:PRK09581  84 ALDDPEDRVRGLEAGADDFLTKP 106
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
522-622 1.11e-09

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: 56.23  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAED-VESSYLQINAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAITAY 600
Cdd:cd19939    1 RILIVEDeLELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVREHS-HVPILMLTAR 79
                         90       100
                 ....*....|....*....|..
gi 794205150 601 AFCPEGERALEAGCNEVIAKPY 622
Cdd:cd19939   80 TEEMDRVLGLEMGADDYLCKPF 101
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
521-622 1.32e-09

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 56.10  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIR--AISQEIPIIAI 597
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAgFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKrdEMTRDIPIIML 80
                         90       100
                 ....*....|....*....|....*
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKPY 622
Cdd:cd17618   81 TARGEEEDKVRGLEAGADDYITKPF 105
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
523-631 1.75e-09

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 56.05  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEgYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHG 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17572   81 SVDIAVEAMRLGAYDFLEKPFDADRLRVTV 110
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
396-495 2.71e-09

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: 54.74  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 396 VTQVLFNFLSNAIK---NTIEGSITFGLvkeeEWVKLYVTDTGCGISKEKLPLIFTRFEKLND----FVQGTGLGLPICK 468
Cdd:cd16939    1 MARALDNLLRNALRyahRTVRIALLVSG----GRLTLIVEDDGPGIPAAARERVFEPFVRLDPsrdrATGGFGLGLAIVH 76
                         90       100
                 ....*....|....*....|....*...
gi 794205150 469 SIVERLGGRIEV-ESELGqGSTFILYLP 495
Cdd:cd16939   77 RVALWHGGHVECdDSELG-GACFRLTWP 103
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
521-635 2.80e-09

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: 55.38  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAIS--QEIPIIAI 597
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAgYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPayKFTPILML 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 794205150 598 TAyafcpEGERAL-----EAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17562   81 TT-----ESSDEKkqegkAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
522-634 2.83e-09

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: 55.33  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDvESSYLQIN-AFLKKE---YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:cd19925    2 NVLIVED-DPMVAEIHrAYVEQVpgfTVIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETY 634
Cdd:cd19925   81 TAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
396-495 3.41e-09

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 54.71  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 396 VTQVLFNFLSNA------------IKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFekLNDFVQGTGLG 463
Cdd:cd16918    1 LIQVFLNLVRNAaqalagsggeiiLRTRTQRQVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM--VSGRENGTGLG 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 794205150 464 LPICKSIVERLGGRIEVESELGQgSTFILYLP 495
Cdd:cd16918   79 LAIAQNIVSQHGGVIECDSQPGH-TVFSVSLP 109
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
392-492 4.64e-09

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: 54.39  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 392 DRNRVTQVLFNFLSNAIKNTIEGSITFGLVK-EEEWVKLYVTDTGCGISKEKLPL---IFTRFEKLNDFVQGTGLGLPIC 467
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTVSISIYdEEEYLYFEIWDNGHGFSEQDLKKaleLFYRDDTSRRSGGHYGMGLYIA 80
                         90       100
                 ....*....|....*....|....*
gi 794205150 468 KSIVERLGGRIEVESELGQGSTFIL 492
Cdd:cd16975   81 KNLVEKHGGSLIIENSQKGGAEVTV 105
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
521-574 5.52e-09

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: 52.19  E-value: 5.52e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 794205150   521 KKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMP 574
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEgYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
514-622 6.37e-09

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 57.00  E-value: 6.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 514 MGVENRQKKILIAEDVES------SYLQinaflKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA 587
Cdd:PRK10710   4 LPIDENTPRILIVEDEPKlgqlliDYLQ-----AASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 794205150 588 ISqEIPIIAITAYAfcPEGER--ALEAGCNEVIAKPY 622
Cdd:PRK10710  79 FS-DIPIVMVTAKI--EEIDRllGLEIGADDYICKPY 112
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
551-632 7.09e-09

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 54.14  E-value: 7.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKET 630
Cdd:cd17537   32 SASAFLAAAPPDQPGCLVLDVRMPGMSGLELQDELLARGSNIPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDA 111

                 ..
gi 794205150 631 IE 632
Cdd:cd17537  112 IE 113
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
419-495 8.71e-09

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 58.27  E-value: 8.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 419 GLVKEEEWVKLyvTDtgcgisKEKLPLIF-----TRfEKLNDfVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILY 493
Cdd:COG0643  346 GLITAEEAAAL--SD------EELLELIFapgfsTA-EEVTD-LSGRGVGMDVVKTNIEALGGTIEIESEPGKGTTFTLR 415

                 ..
gi 794205150 494 LP 495
Cdd:COG0643  416 LP 417
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
551-627 9.35e-09

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: 53.90  E-value: 9.35e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17615   31 DGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEV 107
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
522-585 1.12e-08

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: 53.74  E-value: 1.12e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 794205150 522 KILIAEDVESSYLQINAFLKKEYTILWV---PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKI 585
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAEPDIEVVgeaADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
286-485 1.14e-08

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 57.72  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 286 LANMSHEIRTPLNaiVGFSEIIAL-TEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSGLVDEV 364
Cdd:PRK10815 270 LTDLTHSLKTPLA--VLQSTLRSLrSGKQMSVEQAEPIMLEQISRISQQIGYYLHRASMRSEHNLLSRELHSVAPLLDNL 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 365 ----DKVHRlkmKKGVKLNVIRPSEEIWIStDRNRVTQVLFNFLSNAIK---NTIEGSITFGlvkeEEWVKLYVTDTGCG 437
Cdd:PRK10815 348 tsalNKVYQ---RKGVNITLDISPEITFVG-EKNDFMEVMGNVLDNACKyclEFVEISARQT----DEHLHIVVEDDGPG 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 794205150 438 ISKEKLPLIFTRFEKLNDFVQGTGLGLPICKSIVERLGGRIEV-ESELG 485
Cdd:PRK10815 420 IPESKRELIFDRGQRADTLRPGQGLGLSVAREITEQYEGKISAgDSPLG 468
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
523-627 1.16e-08

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: 53.44  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAgYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRATPVLILTARD 80
                         90       100
                 ....*....|....*....|....*.
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd19934   81 SWQDKVEGLDAGADDYLTKPFHIEEL 106
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
523-627 1.43e-08

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: 53.26  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVE--SSYLQINafLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd17624    1 ILLVEDDAllGDGLKTG--LRKAgYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQSLPVLILTA 78
                         90       100
                 ....*....|....*....|....*...
gi 794205150 600 YAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17624   79 RDGVDDRVAGLDAGADDYLVKPFALEEL 106
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
402-495 1.48e-08

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


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 52.71  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 402 NFLSNAIK---NTIEGSITfglVKEEEWVkLYVTDTGCGISKEKLPLIFTRFEKLNDFVQ----GTGLGLPICKSIVERL 474
Cdd:cd16949    7 NVLRNALRyspSKILLDIS---QDGDQWT-ITITDDGPGVPEDQLEQIFLPFYRVDSARDresgGTGLGLAIAERAIEQH 82
                         90       100
                 ....*....|....*....|.
gi 794205150 475 GGRIEVESELGQGSTFILYLP 495
Cdd:cd16949   83 GGKIKASNRKPGGLRVRIWLP 103
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
399-495 1.64e-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: 52.39  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 399 VLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDF--VQGTGLGLPICKSIVERLG 475
Cdd:cd16923    4 VFSNLLSNAIKYSPENTrIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSrnTEGAGLGLSIAKAIIELHG 83
                         90       100
                 ....*....|....*....|
gi 794205150 476 GRIEVESElGQGSTFILYLP 495
Cdd:cd16923   84 GSASAEYD-DNHDLFKVRLP 102
PRK15115 PRK15115
response regulator GlrR; Provisional
544-635 2.25e-08

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 56.77  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 544 YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYP 623
Cdd:PRK15115  30 YSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQKVQPGMPVIILTAHGSIPDAVAATQQGVFSFLTKPVD 109
                         90
                 ....*....|..
gi 794205150 624 LEKLKETIETYL 635
Cdd:PRK15115 110 RDALYKAIDDAL 121
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
523-621 2.52e-08

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 51.82  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAITAYA 601
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEgFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN-VPVIMVTAKD 79
                         90       100
                 ....*....|....*....|
gi 794205150 602 FCPEGERALEAGCNEVIAKP 621
Cdd:cd17621   80 SEIDKVVGLELGADDYVTKP 99
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
523-622 2.72e-08

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: 52.31  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVE-----SSYLQINAFlkkeyTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAI 597
Cdd:cd17623    2 LLIDDDREltellTEYLEMEGF-----NVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ-VPVLML 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 598 TAyafcpEGER-----ALEAGCNEVIAKPY 622
Cdd:cd17623   76 TA-----RGDDidrilGLELGADDYLPKPF 100
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
521-632 2.82e-08

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: 52.41  E-value: 2.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDVES--SYLQiNAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:cd17569    1 PTILLVDDEPNilKALK-RLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLT 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 794205150 599 AYAfcpEGERALEAgCNEV-----IAKPYPLEKLKETIE 632
Cdd:cd17569   80 GYA---DLDAAIEA-INEGeiyrfLTKPWDDEELKETIR 114
PAS COG2202
PAS domain [Signal transduction mechanisms];
54-268 2.99e-08

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 55.03  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  54 ILGLKEAGIIFRDINDFYrfaHPEDVISYQTTFARMLESEtKISQIVVRCVGRQGETIWLEDNFIAYKkNKENGSDKIIA 133
Cdd:COG2202   43 LTGYSAEELLGKTLRDLL---PPEDDDEFLELLRAALAGG-GVWRGELRNRRKDGSLFWVELSISPVR-DEDGEITGFVG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 134 YTANITSRCEKEAQIRQLEERNRKIIEALPEFIFIFDDNFFITDVLMAPDTELLHPVEVLKGADGRSIYSSEVSDLFISS 213
Cdd:COG2202  118 IARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL 197
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 794205150 214 IHECLKSG-KLKEIEYPV-DVEAGRHFFQARIAPFEGNK----VLALIHDIGDRMRRSQEL 268
Cdd:COG2202  198 LRRLLEGGrESYELELRLkDGDGRWVWVEASAVPLRDGGevigVLGIVRDITERKRAEEAL 258
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
550-632 3.38e-08

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 53.95  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 550 PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKE 629
Cdd:COG4566   30 ASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALLD 109

                 ...
gi 794205150 630 TIE 632
Cdd:COG4566  110 AVR 112
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-495 5.35e-08

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


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 51.42  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNT--IEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRF----EKLNDFVQGTGLGLPICKSIV 471
Cdd:cd16953    3 QVLRNLIGNAISFSppDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFyterPANEAFGQHSGLGLSISRQII 82
                         90       100
                 ....*....|....*....|....*...
gi 794205150 472 ERLGGRIEVES----ELGQGSTFILYLP 495
Cdd:cd16953   83 EAHGGISVAENhnqpGQVIGARFTVQLP 110
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
392-495 5.65e-08

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: 51.38  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 392 DRNRVTQVLFNFLSNAIKNTIEGSITFGLVK------EEEWVKLYVTDTGCGISKEKLPLIFTRFekLNDFVQGTGLGLP 465
Cdd:cd16944    1 DTTQISQVLTNILKNAAEAIEGRPSDVGEVRirveadQDGRIVLIVCDNGKGFPREMRHRATEPY--VTTRPKGTGLGLA 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 466 ICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16944   79 IVKKIMEEHGGRISLSNREAGGACIRIILP 108
envZ PRK09467
osmolarity sensor protein; Provisional
277-480 5.66e-08

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 55.69  E-value: 5.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 277 EADRmkSVFLANMSHEIRTPLNAIVGFSEIIAltedekEKEEYL--GIIQ--QNSNlllQLINDILDLSRIESgksEMHC 352
Cdd:PRK09467 226 EDDR--TLLMAGVSHDLRTPLTRIRLATEMMS------EEDGYLaeSINKdiEECN---AIIEQFIDYLRTGQ---EMPM 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 353 QLTEMSGLVDEV-------DKVHRLKMKKGVKLNVIRPseeiwISTDRnrvtqVLFNFLSNAIKNTiEGSITFGLVKEEE 425
Cdd:PRK09467 292 EMADLNALLGEViaaesgyEREIETALQPGPIEVPMNP-----IAIKR-----ALANLVVNAARYG-NGWIKVSSGTEGK 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 794205150 426 WVKLYVTDTGCGISKEKLPLIFtrfeklNDFVQG--------TGLGLPICKSIVERLGGRIEV 480
Cdd:PRK09467 361 RAWFQVEDDGPGIPPEQLKHLF------QPFTRGdsargssgTGLGLAIVKRIVDQHNGKVEL 417
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
523-627 6.05e-08

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: 51.23  E-value: 6.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAITAYA 601
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEgYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQS-EVGIILVTGRD 81
                         90       100
                 ....*....|....*....|....*.
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17619   82 DEVDRIVGLEIGADDYVTKPFNPREL 107
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-480 6.71e-08

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 50.92  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNTIE-GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKL---NDFVQGTGLGLPICKSIVER 473
Cdd:cd16945    7 QAINNLLDNAIDFSPEgGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSLprpHSGQKSTGLGLAFVQEVAQL 86

                 ....*..
gi 794205150 474 LGGRIEV 480
Cdd:cd16945   87 HGGRITL 93
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
520-621 7.19e-08

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


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 52.61  E-value: 7.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 520 QKKILIAEDvESSYLQI--NAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:COG4567    4 DRSLLLVDD-DEAFARVlaRALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPDARIVVL 82
                         90       100
                 ....*....|....*....|....
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKP 621
Cdd:COG4567   83 TGYASIATAVEAIKLGADDYLAKP 106
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
522-622 1.11e-07

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 50.45  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAED------VESSYLQINAFlkkEYTILWvpNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPII 595
Cdd:cd19938    1 RILIVEDepklaqLLIDYLRAAGY---APTLLA--HGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFS-DVPII 74
                         90       100
                 ....*....|....*....|....*....
gi 794205150 596 AITAYAfcPEGER--ALEAGCNEVIAKPY 622
Cdd:cd19938   75 MVTARV--EEIDRllGLELGADDYICKPY 101
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
419-495 1.82e-07

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: 51.43  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 419 GLVKEEEWVKLyvTDtgcgisKEKLPLIF-----TRfEKLNDfVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILY 493
Cdd:cd16916  107 GLITADEAATL--SD------DEVLNLIFapgfsTA-EQVTD-VSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIR 176

                 ..
gi 794205150 494 LP 495
Cdd:cd16916  177 LP 178
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
521-601 1.83e-07

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: 49.75  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDvESSYLQI--NAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:cd17563    1 KSLLLVDD-DEVFAERlaRALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLRALQPDARIVVLT 79

                 ...
gi 794205150 599 AYA 601
Cdd:cd17563   80 GYA 82
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
266-495 2.03e-07

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 53.78  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 266 QELLEAKQRaeeadrmksvFLANMSHEIRTPL------NAI----VGFSEIIALTEDEKEKeeylgiiqqnsnlLLQLIN 335
Cdd:PRK09470 237 ERMMTSQQR----------LLSDISHELRTPLtrlqlaTALlrrrQGESKELERIETEAQR-------------LDSMIN 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 336 DILDLSRIESgKSEMHCQLTEMSGLVDEVDKVHRLKMKK-GVKLNVIRPSEEIWISTDRNRVTQVLFNFLSNAIK---NT 411
Cdd:PRK09470 294 DLLVLSRNQQ-KNHLERETFKANSLWSEVLEDAKFEAEQmGKSLTVSAPPGPWPINGNPNALASALENIVRNALRyshTK 372
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 412 IEGSITfglVKEEEwVKLYVTDTGCGISKEKLPLIFTRFEKlndfVQ--------GTGLGLPICKSIVERLGGRIEVE-S 482
Cdd:PRK09470 373 IEVAFS---VDKDG-LTITVDDDGPGVPEEEREQIFRPFYR----VDeardresgGTGLGLAIVENAIQQHRGWVKAEdS 444
                        250
                 ....*....|...
gi 794205150 483 ELGqGSTFILYLP 495
Cdd:PRK09470 445 PLG-GLRLTIWLP 456
PRK09191 PRK09191
two-component response regulator; Provisional
553-631 2.27e-07

two-component response regulator; Provisional


Pssm-ID: 236402 [Multi-domain]  Cd Length: 261  Bit Score: 52.54  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 553 EEAVKSFIREKPDLILMDIRM-PVMNGIQATAKIRAiSQEIPIIAITAYafcPE----GERAleagcnE---VIAKPYPL 624
Cdd:PRK09191 172 AEAVALAKKTRPGLILADIQLaDGSSGIDAVNDILK-TFDVPVIFITAF---PErlltGERP------EpafLITKPFQP 241

                 ....*..
gi 794205150 625 EKLKETI 631
Cdd:PRK09191 242 DTVKAAI 248
PRK09483 PRK09483
response regulator; Provisional
550-613 2.97e-07

response regulator; Provisional


Pssm-ID: 236538 [Multi-domain]  Cd Length: 217  Bit Score: 51.65  E-value: 2.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 794205150 550 PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAG 613
Cdd:PRK09483  34 CCGEDAVKWCRTNAVDVVLMDMNMPGIGGLEATRKILRYTPDVKIIMLTVHTENPLPAKVMQAG 97
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
399-495 3.55e-07

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: 50.42  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 399 VLFNFLSNAIKNTIEGSITFG---------LVKEEEWVKLYVTDTGCGISKEKLPLIF-----TRFEKLND--------- 455
Cdd:cd16929   47 ILFELLKNAMRATVESHGDDSddlppikvtVAKGDEDLTIKISDRGGGIPREDLARLFsymysTAPQPSLDdfsdlisgt 126
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 794205150 456 ---FVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYLP 495
Cdd:cd16929  127 qpsPLAGFGYGLPMSRLYAEYFGGDLDLQSMEGYGTDVYIYLK 169
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
398-495 5.68e-07

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 48.21  E-value: 5.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 398 QVLFNFLSNAIKNTiEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLI---FTRFEKLNDfVQGTGLGLPICKSIVERL 474
Cdd:cd16950    3 RVLSNLVDNALRYG-GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELfqpFYRGDNARG-TSGTGLGLAIVQRISDAH 80
                         90       100
                 ....*....|....*....|.
gi 794205150 475 GGRIEVESELGQGSTFILYLP 495
Cdd:cd16950   81 GGSLTLANRAGGGLCARIELP 101
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
285-495 6.22e-07

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: 52.44  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  285 FLANMS----HEIRTPLnAIVGFS-EIIALTEDEKEKEEYLGIIQQNSNLLLQLINDILDLSRIESGKSEMHCQLTEMSG 359
Cdd:TIGR03785 484 YLENMSsrlsHELRTPV-AVVRSSlENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSE 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  360 LVDE-------VDKVHRLKMKKGVKLNVIRPSEEIwistdrnrVTQVLFNFLSNAIKNTIEGS-ITFGLVKEEEWVKLYV 431
Cdd:TIGR03785 563 VLSGcmqgyqmTYPPQRFELNIPETPLVMRGSPEL--------IAQMLDKLVDNAREFSPEDGlIEVGLSQNKSHALLTV 634
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150  432 TDTGCGIS---KEKL--PLIFTRFEKLNDfVQGTGLGLPICKSIVERLGGRIEVESEL-GQGSTFILYLP 495
Cdd:TIGR03785 635 SNEGPPLPedmGEQLfdSMVSVRDQGAQD-QPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
406-498 8.10e-07

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 51.94  E-value: 8.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 406 NAIKNTIE-----GSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTRFEKLNDfvqGTGLGLpicKSIVERL------ 474
Cdd:COG2972  347 NAIEHGIEpkeggGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGE---GRGIGL---RNVRERLklyyge 420
                         90       100
                 ....*....|....*....|....
gi 794205150 475 GGRIEVESELGQGSTFILYLPNRQ 498
Cdd:COG2972  421 EYGLEIESEPGEGTTVTIRIPLEE 444
ompR PRK09468
osmolarity response regulator; Provisional
518-627 8.74e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 50.36  E-value: 8.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 518 NRQKKILIAED------VESSYLQinaflKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQE 591
Cdd:PRK09468   3 QENYKILVVDDdmrlraLLERYLT-----EQGFQVRSAANAEQMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNP 77
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 794205150 592 IPIIAITAYAfcPEGER--ALEAGCNEVIAKPY-PLEKL 627
Cdd:PRK09468  78 TPIIMLTAKG--EEVDRivGLEIGADDYLPKPFnPRELL 114
fixJ PRK09390
response regulator FixJ; Provisional
554-635 1.57e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 49.23  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 554 EAVKSFIREKPDL----ILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKE 629
Cdd:PRK09390  34 ESAQAFLDALPGLrfgcVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGDVPLAVEAMKLGAVDFIEKPFEDERLIG 113

                 ....*.
gi 794205150 630 TIETYL 635
Cdd:PRK09390 114 AIERAL 119
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
523-621 1.71e-06

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: 46.99  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAED-VESSYLQINAFLKKEYTILWVPNGEEAVKSF---------IREKPDLILMDIRMPVMNGIQATAKIRA--ISQ 590
Cdd:cd19924    1 ILVVDDsPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDdpRLA 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 794205150 591 EIPIIAITAYAFCPEGERALEAGCNEVIAKP 621
Cdd:cd19924   81 NIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
404-501 2.09e-06

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


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 50.67  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 404 LSNAIK----NTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKlpliftrfeklnDFVQGTGLGLPICKSIVERLGGRIE 479
Cdd:COG3920  408 VTNALKhaflSGEGGRIRVSWRREDGRLRLTVSDNGVGLPEDV------------DPPARKGLGLRLIRALVRQLGGTLE 475
                         90       100
                 ....*....|....*....|..
gi 794205150 480 VESElgQGSTFILYLPNRQVQE 501
Cdd:COG3920  476 LDRP--EGTRVRITFPLAELAA 495
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
522-627 2.50e-06

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: 46.62  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKK---EYTIlwVPNGEEAVKSFIREKPD--LILMDIRMPVMNGIQATAKIRAI--SQEIP- 593
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKlgcEVTT--VSSGEECLNLLASAEHSfqLVLLDLCMPEMDGFEVALRIRKLfgRRERPl 79
                         90       100       110
                 ....*....|....*....|....*....|....
gi 794205150 594 IIAITAYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd19933   80 IVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
523-631 3.35e-06

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: 46.98  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAF 602
Cdd:cd17596    3 ILVVDDEVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIIISGYTD 82
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 603 CPEGERAL-EAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17596   83 SEDIIAGInEAGIYQYLTKPWHPDQLLLTV 112
PRK11517 PRK11517
DNA-binding response regulator HprR;
522-627 3.62e-06

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 48.36  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEiPIIAITAY 600
Cdd:PRK11517   2 KILLIEDNQRTQEWVTQGLSEAgYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQT-PVICLTAR 80
                         90       100
                 ....*....|....*....|....*..
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:PRK11517  81 DSVDDRVRGLDSGANDYLVKPFSFSEL 107
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
535-621 3.87e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 45.82  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 535 QINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQ--EIPIIAITAYAFCPEGERALE 611
Cdd:cd17602   13 MIEYFLEKQgFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTGKDGLVDRIRAKM 92
                         90
                 ....*....|
gi 794205150 612 AGCNEVIAKP 621
Cdd:cd17602   93 AGASGYLTKP 102
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
251-495 3.97e-06

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 48.85  E-value: 3.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 251 VLALIHDIGDRMRRSQEL----LEAKQRAEEADRMK-----------SVFLANMSheirtpLNAIvgfseIIALTEDEKE 315
Cdd:COG4585   21 LLALVLLRARRAERAAELerelAARAEEAREEERRRiarelhdgvgqSLSAIKLQ------LEAA-----RRLLDADPEA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 316 KEEYLGIIQQNSNLLLQLINDILdlsriesgkSEMHCQLTEMSGLVDEVDK-VHRLKMKKGVKLNVIRPSEEIWISTDRN 394
Cdd:COG4585   90 AREELEEIRELAREALAELRRLV---------RGLRPPALDDLGLAAALEElAERLLRAAGIRVELDVDGDPDRLPPEVE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 395 ----RVTQVLfnfLSNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPliftrfeklndfvqGTGLGLpicKSI 470
Cdd:COG4585  161 lalyRIVQEA---LTNALKHAGATRVTVTLEVDDGELTLTVRDDGVGFDPEAAP--------------GGGLGL---RGM 220
                        250       260
                 ....*....|....*....|....*...
gi 794205150 471 VER---LGGRIEVESELGQGSTFILYLP 495
Cdd:COG4585  221 RERaeaLGGTLTIGSAPGGGTRVRATLP 248
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
523-621 4.20e-06

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: 45.51  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDvE---SSYLQINafLKKE-YTILWVPNGEEAvKSFIREKP-DLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:cd19935    1 ILVVED-EkklAEYLKKG--LTEEgYAVDVAYDGEDG-LHLALTNEyDLIILDVMLPGLDGLEVLRRLRAAGKQTPVLML 76
                         90       100
                 ....*....|....*....|....
gi 794205150 598 TAYAFCPEGERALEAGCNEVIAKP 621
Cdd:cd19935   77 TARDSVEDRVKGLDLGADDYLVKP 100
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
522-622 5.22e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.26  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVkSFIREKPDLILMDIRMPVMNGIQATAKIRAiSQEIPIIAITAY 600
Cdd:PRK10955   3 KILLVDDDRELTSLLKELLEMEgFNVIVAHDGEQAL-DLLDDSIDLLLLDVMMPKKNGIDTLKELRQ-THQTPVIMLTAR 80
                         90       100
                 ....*....|....*....|....
gi 794205150 601 AfcPEGER--ALEAGCNEVIAKPY 622
Cdd:PRK10955  81 G--SELDRvlGLELGADDYLPKPF 102
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
404-495 8.39e-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: 44.47  E-value: 8.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 404 LSNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGISKEKLPliftrfeklndfvQGTGLGLPICKSIVERLGGRIEVESE 483
Cdd:cd16917    9 LTNALKHAGASRVRVTLSYTADELTLTVVDDGVGFDGPAPP-------------GGGGFGLLGMRERAELLGGTLTIGSR 75
                         90
                 ....*....|..
gi 794205150 484 LGQGSTFILYLP 495
Cdd:cd16917   76 PGGGTRVTARLP 87
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
550-628 9.39e-06

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: 44.93  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 550 PNGEEAVkSFIREKP---DLILMDIRMPVMNGIQATAKIRAISqEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEK 626
Cdd:cd17584   29 TDAEEAL-SMLRENKdefDLVITDVHMPDMDGFEFLELIRLEM-DLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIED 106

                 ..
gi 794205150 627 LK 628
Cdd:cd17584  107 LK 108
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
565-627 9.51e-06

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 44.73  E-value: 9.51e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 794205150 565 DLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17573   44 DLVLVSDKLPDGNGLSIVSRIKEKHPSIVVIVLSDNPKTEQEIEAFKEGADDYIAKPFDFKVL 106
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
551-599 1.21e-05

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 44.36  E-value: 1.21e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAITA 599
Cdd:cd19936   30 DGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQKST-LPVIFLTS 77
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
521-635 1.24e-05

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 47.02  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 521 KKILIAEDvESSYLQINAFLKKE--YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIR--AISQEIPIIA 596
Cdd:PRK10161   3 RRILVVED-EAPIREMVCFVLEQngFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKreSMTRDIPVVM 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 794205150 597 ITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:PRK10161  82 LTARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVM 120
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
522-635 1.81e-05

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 44.53  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVES--SYLQ--INAFLKK---EYTILWVPNGEE---AVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQE 591
Cdd:cd17533    2 NIFILEDDKIqrVRLEeiIENILKIeniEYVIELTGKTEElleKIKERGKNGIYFLDIDIKMEEKNGLEVAQKIRKYDPY 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 794205150 592 IPIIAITAYA-FCPEG-ERALEAgcNEVIAKPYPLEKLKETIETYL 635
Cdd:cd17533   82 AIIIFVTTHSeFAPLTfEYKVAA--LDFILKPLKLEEFKKRIEECI 125
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
522-622 2.26e-05

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: 43.75  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAED------VESSYLQinafLKKEYTILWV-PNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRA--ISQEI 592
Cdd:cd17561    3 KVLIADDnrefvqLLEEYLN----SQPDMEVVGVaHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRmrLEKRP 78
                         90       100       110
                 ....*....|....*....|....*....|
gi 794205150 593 PIIAITAYAFCPEGERALEAGCNEVIAKPY 622
Cdd:cd17561   79 KIIMLTAFGQEDITQRAVELGASYYILKPF 108
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
554-632 2.73e-05

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


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 43.78  E-value: 2.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 554 EAVKSFIREKPDLILMDIRMP-VMNGIQATAKIRAiSQEIPIIAITAYafcPE----GERALEAgcnEVIAKPYPLEKLK 628
Cdd:cd17540   36 EAVALARRERPDLILADIQLAdGSSGIDAVNEILT-THDVPVIFVTAY---PErlltGERPEPT---FLITKPFDPEMVK 108

                 ....
gi 794205150 629 ETIE 632
Cdd:cd17540  109 AAIS 112
PRK10766 PRK10766
two-component system response regulator TorR;
520-627 2.76e-05

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 45.80  E-value: 2.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 520 QKKILIAEDVESSYLQINAFLKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISqEIPIIAIT 598
Cdd:PRK10766   2 SYHILVVEDEPVTRARLQGYFEQEgYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELRSRS-TVGIILVT 80
                         90       100
                 ....*....|....*....|....*....
gi 794205150 599 AYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:PRK10766  81 GRTDSIDRIVGLEMGADDYVTKPLELREL 109
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
551-598 4.04e-05

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 45.02  E-value: 4.04e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:PRK10651  40 NGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGRIVVFS 87
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
520-622 4.64e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 45.34  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 520 QKKILIAEDvESSYLQINAF-LKKE-YTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAI 597
Cdd:PRK11083   3 QPTILLVED-EQAIADTLVYaLQSEgFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFL 81
                         90       100
                 ....*....|....*....|....*..
gi 794205150 598 TAYAfcPEGER--ALEAGCNEVIAKPY 622
Cdd:PRK11083  82 TARS--DEVDRlvGLEIGADDYVAKPF 106
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
548-621 5.19e-05

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


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 42.49  E-value: 5.19e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 794205150 548 WVPNGEEavksfirekpDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKP 621
Cdd:cd19928   37 WVEEGEG----------DLVITDVVMPDENGLDLIPRIKKARPDLPIIVMSAQNTLMTAVKAAERGAFEYLPKP 100
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
522-631 5.76e-05

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: 42.82  E-value: 5.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAED------VESSYLQINAFLKKEytilwVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQeIPII 595
Cdd:cd17594    1 HVLVVDDdaamrhLLILYLRERGFDVTA-----AADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSD-VPII 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 794205150 596 AITAYAFcPEGER--ALEAGCNEVIAKPYPLEKLKETI 631
Cdd:cd17594   75 IISGDRR-DEIDRvvGLELGADDYLAKPFGLRELLARV 111
PRK15369 PRK15369
two component system response regulator;
522-633 7.08e-05

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 44.30  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAEDVEssyLQINAFLK-----KEYTIL-WVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPII 595
Cdd:PRK15369   5 KILLVDDHE---LIINGIKNmlapyPRYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLHQRWPAMNIL 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 794205150 596 AITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETIET 633
Cdd:PRK15369  82 VLTARQEEHMASRTLAAGALGYVLKKSPQQILLAAIQT 119
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
551-632 7.78e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 45.63  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKET 630
Cdd:PRK10923  35 NGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPMLPVIIMTAHSDLDAAVSAYQQGAFDYLPKPFDIDEAVAL 114

                 ..
gi 794205150 631 IE 632
Cdd:PRK10923 115 VE 116
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
522-635 9.53e-05

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.14  E-value: 9.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 522 KILIAED-VESSYLQINAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAY 600
Cdd:PRK09836   2 KLLIVEDeKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTAL 81
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 794205150 601 AFCPEGERALEAGCNEVIAKPYPLEKLKETIETYL 635
Cdd:PRK09836  82 GTIEHRVKGLELGADDYLVKPFAFAELLARVRTLL 116
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
346-495 1.25e-04

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 45.21  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 346 GKSEMHCQLTEM----------SGLVdeVDKVHRLKmKKGVKLNVIRPSE--EIWISTDRNRVTQVLFNFLSNAIKNTI- 412
Cdd:PRK15053 374 GESQAQQQLIDSlreafadrqvAGLL--FGKVQRAR-ELGLKMVIVPGSQlsQLPPGLDSTEFAAIVGNLLDNAFEASLr 450
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 413 ----EGSITFGLVKEEEWVKLYVTDTGCGISKEKLPLIFTR-FEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQG 487
Cdd:PRK15053 451 sdegNKIVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQgVSTRADEPGEHGIGLYLIASYVTRCGGVITLEDNDPCG 530

                 ....*...
gi 794205150 488 STFILYLP 495
Cdd:PRK15053 531 TLFSIFIP 538
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
388-494 1.38e-04

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: 42.06  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 388 WISTDRNRVTQVLFNFLSNAIKNTIE-GSITF--------GLVKEEEW-------------VKLYVTDTGCGISKEKLPL 445
Cdd:cd16938    4 VVVGDERRVFQVLLHMLGNLLKMRNGgGNITFrvfleggsEDRSDRDWgpwrpsmsdesveIRFEVEINDSGSPSIESAS 83
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 794205150 446 IF-TRFEKLNDFVQGTGLGLPICKSIVERLGGRIEVESELGQGSTFILYL 494
Cdd:cd16938   84 MRnSLNRRYNLSELGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLLL 133
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
549-598 1.68e-04

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 41.56  E-value: 1.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 794205150 549 VPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAIT 598
Cdd:cd19931   30 ASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREEGVSARIVILT 79
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
544-622 1.68e-04

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: 41.18  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 544 YTILWVPNGEEAVKSFIRE-KPDLILMDIRMP-VMNGIQATAKIRAISQEIPIIAITAYAfcpegERALEAGCN----EV 617
Cdd:cd18161   23 YTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSGYA-----ENAIEGGDLapgvDV 97

                 ....*
gi 794205150 618 IAKPY 622
Cdd:cd18161   98 LSKPF 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
523-595 1.98e-04

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: 40.85  E-value: 1.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 794205150 523 ILIAEDVESSYLQINAFLKK-EYTILWVPNGEEAVKSFIREKP--DLILMDIRMPVMNGIQATAKI--RAISQEIPII 595
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKcSYEVTAASDGLQAWDVLEDEQNeiDLILTEVDLPVSSGFKLLSYImrHKICKNIPVI 78
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
525-627 2.30e-04

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 41.55  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 525 IAEDVESSYlqinaflKKEYTILWVPNGEEAVKSF--IREKPD---LILMDIRMPVMNGIQATAKIRAISQEIPIIAITA 599
Cdd:cd17595   16 VARDLRRQY-------GKDYRVLRADSGAEALDALkeLKLRGEavaLFLVDQRMPEMDGVEFLEKAMELFPEAKRVLLTA 88
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 794205150 600 YAfcpEGERALEAgCNEV-----IAKPY--PLEKL 627
Cdd:cd17595   89 YA---DTDAAIRA-INDVqldyyLLKPWdpPEEKL 119
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
49-134 3.68e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 39.63  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150   49 DEYFHILGLKEAGIIfRDINDFYRFAHPEDVISYQTTFARMLESETKISqIVVRCVGRQGETIWLEDNFIAYkKNKENGS 128
Cdd:pfam08447   6 PRFEEILGYTPEELL-GKGESWLDLVHPDDRERVREALWEALKGGEPYS-GEYRIRRKDGEYRWVEARARPI-RDENGKP 82

                  ....*.
gi 794205150  129 DKIIAY 134
Cdd:pfam08447  83 VRVIGV 88
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
551-632 4.88e-04

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 41.80  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKET 630
Cdd:PRK09958  33 EGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIVSAKNDHFYGKHCADAGANGFVSKKEGMNNIIAA 112

                 ..
gi 794205150 631 IE 632
Cdd:PRK09958 113 IE 114
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
551-621 7.03e-04

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 39.44  E-value: 7.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 794205150 551 NGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAKP 621
Cdd:cd19926   30 NVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQRLPQTPVAVITAYGSLDTAIEALKAGAFDFLTKP 100
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
523-627 1.02e-03

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: 39.31  E-value: 1.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKEYTILWVPN-GEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYA 601
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDlGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSGLA 80
                         90       100
                 ....*....|....*....|....*.
gi 794205150 602 FCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:cd17616   81 DIEDKVKGLGFGADDYMTKPFHKDEL 106
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
563-627 2.14e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.17  E-value: 2.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 794205150 563 KPDLILMDIRMPVMNGIQATAKIRAISQeIPIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKL 627
Cdd:PRK10529  45 KPDLIILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSARSEESDKIAALDAGADDYLSKPFGIGEL 108
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
523-621 3.36e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.06  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 523 ILIAEDVESSYLQINAFLKKEYTILWVPNGEEAVKSFIREKPDLILMDIRMPVMNGIQATAKIRAI--SQEIPIIAItay 600
Cdd:cd17539    1 VLLVDDRPSSAERIAAMLSSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLerTRQLPILAV--- 77
                         90       100
                 ....*....|....*....|....*.
gi 794205150 601 afCPEGE-----RALEAGCNEVIAKP 621
Cdd:cd17539   78 --ADPGDrgrliRALEIGVNDYLVRP 101
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
559-620 3.75e-03

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 39.09  E-value: 3.75e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 794205150 559 FIREKP-DLILMDIRMPVMNGIQATAKIRAISQEIPIIAITAYAFCPEGERALEAGCNEVIAK 620
Cdd:PRK09935  44 YLRTRPvDLIIMDIDLPGTDGFTFLKRIKQIQSTVKVLFLSSKSECFYAGRAIQAGANGFVSK 106
HATPase_EL346-LOV-HK-like cd16951
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
396-495 4.36e-03

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


Pssm-ID: 340427 [Multi-domain]  Cd Length: 131  Bit Score: 37.78  E-value: 4.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 396 VTQVLFNFLSNAIKNTIEGSITFGLVKEEEWVKLYVTDTGCGiskekLPLIFTRFEKLNdfvqgtgLGLPICKSIVERLG 475
Cdd:cd16951   44 VNELLQNALKHAFSDREGGTITIRSVVDGDYLRITVIDDGVG-----LPQDEDWPNKGS-------LGLQIVRSLVEGEL 111
                         90       100
                 ....*....|....*....|
gi 794205150 476 GRIEVESELGQGSTFILYLP 495
Cdd:cd16951  112 KAFLEVQSAENGTRVNIDIP 131
PRK10610 PRK10610
chemotaxis protein CheY;
518-631 8.16e-03

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 36.88  E-value: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 794205150 518 NRQKKILIAEDVeSSYLQINAFLKKEYTILWVPNGEEAVKSFIREKP---DLILMDIRMPVMNGIQATAKIRAISQ--EI 592
Cdd:PRK10610   3 DKELKFLVVDDF-STMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAggfGFVISDWNMPNMDGLELLKTIRADGAmsAL 81
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 794205150 593 PIIAITAYAFCPEGERALEAGCNEVIAKPYPLEKLKETI 631
Cdd:PRK10610  82 PVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH