NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|18421494|ref|NP_568532|]
View 

histidine kinase 2 [Arabidopsis thaliana]

Protein Classification

CHASE and HATPase_EvgS-ArcB-TorS-like domain-containing protein( domain architecture ID 13692917)

protein containing domains CHASE, HisKA, HATPase_EvgS-ArcB-TorS-like, and REC

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
578-1172 5.09e-108

hybrid sensory histidine kinase BarA; Provisional


The actual alignment was detected with superfamily member PRK11107:

Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 361.09  E-value: 5.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   578 KARA-EAADIaKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLEL 656
Cdd:PRK11107  283 KKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   657 ENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTqERGHIFISVHLadevk 736
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFT-ESGNIDILVEL----- 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   737 epltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystESQNSDQIKLLVTVEDTGVGIPVDAQGRIFTPFM 816
Cdd:PRK11107  436 ----------------------------------------------RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   817 QADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTGVFGKAETNTSItklerfDLAIQEFTGLRALVID 896
Cdd:PRK11107  470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIID------GLPTDCLAGKRLLYVE 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   897 NRNIRAEVTRYELRRLGISADIVSSLrmactcciSKLENLA--MILIDKDAWNKEEFSVLDELFTRSKvtfTRVPKIFLL 974
Cdd:PRK11107  544 PNSAAAQATLDILSETPLEVTYSPTL--------SQLPEAHydILLLGLPVTFREPLTMLHERLAKAK---SMTDFLILA 612
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   975 ATSATLTERSEMKSTGlIDEVVIKPLRMSVLICCLQETlvngkkrQPNRQRRNLGHLLREKQ---ILVVDDNLVNrrvae 1051
Cdd:PRK11107  613 LPCHEQVLAEQLKQDG-ADACLSKPLSHTRLLPALLEP-------CHHKQPPLLPPTDESRLpltVMAVDDNPAN----- 679
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1052 gaLKKYGA--------IVTCvESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELerEINKkiasgevsaemfc 1123
Cdd:PRK11107  680 --LKLIGAlleeqvehVVLC-DSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELIRQL--PHNQ------------- 740
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 18421494  1124 kfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:PRK11107  741 -----NTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
304-499 3.52e-43

CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 427591  Cd Length: 184  Bit Score: 155.53  E-value: 3.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    304 SAIDQRTFEEYTERTNFERPLTSGVAYALKVPHSEREKFEKEH------GWAIKkmetedqtvvqdcvpenfdPAPIQDE 377
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR-------------------PAGDRDE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    378 YAPVIFAQETVSH--IVSVDMMSGEEDRENILRARASGKGVLTSPFKLL--KSNHLGVVLTFAVYDTSLPPdaTEEQRVE 453
Cdd:pfam03924   62 YFPIIYIEPLAGNnrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRA 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 18421494    454 ATIGYLGASYDMPSLVEKLLHQLASkQTIAVDVYDTTNTSGLIKMY 499
Cdd:pfam03924  140 ALLGFVYAPFRIDDLLEAALLRLGE-DGLDLALYDGTSASAPELLY 184
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
578-1172 5.09e-108

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 361.09  E-value: 5.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   578 KARA-EAADIaKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLEL 656
Cdd:PRK11107  283 KKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   657 ENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTqERGHIFISVHLadevk 736
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFT-ESGNIDILVEL----- 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   737 epltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystESQNSDQIKLLVTVEDTGVGIPVDAQGRIFTPFM 816
Cdd:PRK11107  436 ----------------------------------------------RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   817 QADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTGVFGKAETNTSItklerfDLAIQEFTGLRALVID 896
Cdd:PRK11107  470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIID------GLPTDCLAGKRLLYVE 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   897 NRNIRAEVTRYELRRLGISADIVSSLrmactcciSKLENLA--MILIDKDAWNKEEFSVLDELFTRSKvtfTRVPKIFLL 974
Cdd:PRK11107  544 PNSAAAQATLDILSETPLEVTYSPTL--------SQLPEAHydILLLGLPVTFREPLTMLHERLAKAK---SMTDFLILA 612
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   975 ATSATLTERSEMKSTGlIDEVVIKPLRMSVLICCLQETlvngkkrQPNRQRRNLGHLLREKQ---ILVVDDNLVNrrvae 1051
Cdd:PRK11107  613 LPCHEQVLAEQLKQDG-ADACLSKPLSHTRLLPALLEP-------CHHKQPPLLPPTDESRLpltVMAVDDNPAN----- 679
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1052 gaLKKYGA--------IVTCvESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELerEINKkiasgevsaemfc 1123
Cdd:PRK11107  680 --LKLIGAlleeqvehVVLC-DSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELIRQL--PHNQ------------- 740
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 18421494  1124 kfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:PRK11107  741 -----NTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
578-1171 5.30e-72

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: 260.10  E-value: 5.30e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    578 KARAEA--ADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLE 655
Cdd:TIGR02956  452 KARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    656 LENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQeRGHIFISVHLAdev 735
Cdd:TIGR02956  532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRVSLN--- 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    736 kepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsDQIKLLVTVEDTGVGIPVDAQGRIFTPF 815
Cdd:TIGR02956  608 ----------------------------------------------------DDSSLLFEVEDTGCGIAEEEQATLFDAF 635
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    816 MQADSstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTgvfgkaetntsitkLErfdlaiqeftglralvi 895
Cdd:TIGR02956  636 TQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFT--------------LP----------------- 682
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    896 dnrniraevtryelrrlgisadivsslrmactccisklenlamilidkdawnkeefsvldelFTRSKvtftrvpkifLLA 975
Cdd:TIGR02956  683 --------------------------------------------------------------LTRGK----------PAE 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    976 TSATLTersemkstgLIDevvIKPLRmsvlicclqetlvngkkrqpnrqrrnlghllrekqILVVDDNLVNRRVAEGALK 1055
Cdd:TIGR02956  691 DSATLT---------VID---LPPQR-----------------------------------VLLVEDNEVNQMVAQGFLT 723
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   1056 KYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELEREINKkiasgevsaemfckfsswhVPILAM 1135
Cdd:TIGR02956  724 RLGHKVTLAESGQSALECFH-QHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNE-------------------VKFIAF 783
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 18421494   1136 TADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:TIGR02956  784 SAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
575-862 6.34e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 237.50  E-value: 6.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  575 RELKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTdLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRL 654
Cdd:COG0642   97 LALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  655 ELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADE 734
Cdd:COG0642  176 ELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGD 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  735 vkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTP 814
Cdd:COG0642  255 --------------------------------------------------------RVRISVEDTGPGIPPEDLERIFEP 278
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18421494  815 FMQADSstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG0642  279 FFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
704-862 1.88e-47

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: 164.59  E-value: 1.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  704 FRQIITNLVGNSIKFTqERGHIFISVHLadevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystE 783
Cdd:cd16922    1 LRQILLNLLGNAIKFT-EEGEVTLRVSL---------------------------------------------------E 28
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  784 SQNSDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16922   29 EEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFT 107
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
304-499 3.52e-43

CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 427591  Cd Length: 184  Bit Score: 155.53  E-value: 3.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    304 SAIDQRTFEEYTERTNFERPLTSGVAYALKVPHSEREKFEKEH------GWAIKkmetedqtvvqdcvpenfdPAPIQDE 377
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR-------------------PAGDRDE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    378 YAPVIFAQETVSH--IVSVDMMSGEEDRENILRARASGKGVLTSPFKLL--KSNHLGVVLTFAVYDTSLPPdaTEEQRVE 453
Cdd:pfam03924   62 YFPIIYIEPLAGNnrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRA 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 18421494    454 ATIGYLGASYDMPSLVEKLLHQLASkQTIAVDVYDTTNTSGLIKMY 499
Cdd:pfam03924  140 ALLGFVYAPFRIDDLLEAALLRLGE-DGLDLALYDGTSASAPELLY 184
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
699-862 2.85e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 115.82  E-value: 2.85e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     699 GDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfkt 778
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD-------------------------------------------- 36
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     779 cystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPFMQADSsTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGST 858
Cdd:smart00387   37 ------------HVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTT 103

                    ....
gi 18421494     859 FSFT 862
Cdd:smart00387  104 FTIT 107
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
304-488 5.77e-30

This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.


Pssm-ID: 215015  Cd Length: 176  Bit Score: 117.44  E-value: 5.77e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     304 SAIDQRTFEEYTERTNFER--PLTSGVAYALKVPHSEREKFEkehgWAIKKMETEDQTVVQDcvpenfdPAPIQDEYAPV 381
Cdd:smart01079    2 ESVSRAEFRRFALELQLNRrlPGIQGLGWAPRVPPAERAAFE----AALRAGGPGLFNIRLA-------PDGERDEYFVI 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     382 IFAQETVSH--IVSVDMMSGEEDRENILRARASGKGVLTSPFKLLKSNH--LGVVLTFAVYDtslpPDATEEQRVEATIG 457
Cdd:smart01079   71 TYIEPLAGNeaALGLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGdgRGFLLRLPVYR----GGPPTSTRREALWG 146
                           170       180       190
                    ....*....|....*....|....*....|.
gi 18421494     458 YLGASYDMPSLVEKLLHQLASKQtIAVDVYD 488
Cdd:smart01079  147 FVSAVFRLDDLLEGLLGALDLPG-LDLALYD 176
CHASE1 COG3614
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
234-600 2.05e-27

Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442832 [Multi-domain]  Cd Length: 588  Bit Score: 119.02  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  234 ILLLGILggVSFSVWWF-WDTNEEIIMKRRETLAnmcDERARVLQDQFNvslNHVHALSILVSTFHHgkiPSAIDQRTFE 312
Cdd:COG3614   17 VLLLGLL--LTALAWWAvRRAEEQRARARFERLA---DELASALEERLD---AYEQVLRGLAGLFAA---SDDVTRAEFR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  313 EYTERTNFERPLTS--GVAYALKVPHSEREKFEkehgwaikkmetedQTVVQDCVPeNFD--PAPIQDEYAPVIF---AQ 385
Cdd:COG3614   86 RYVASLDLLRRYPGiqGLGWAPRVPAAERAAFE--------------AAARAEGFP-DFRirPAGERDEYFPITYiepLD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  386 ETVSHIVSVDMMSGEEDRENILRARASGKGVLTSPFKLL--KSNHLGVVLTFAVYDTSLPPDaTEEQRVEATIGYLGASY 463
Cdd:COG3614  151 ARNRRALGFDMASEPVRRAAMERARDTGRPAASGPVTLVqeTDGQPGFLLYLPVYRGGAPPD-TVAERRAALRGFVYAPF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  464 DMPSLVEKLLHQLASkQTIAVDVYDTTNTSGLIKMYGSEIGDISE-----QHISSLDFGDpsRNHEMHCR------FKHK 532
Cdd:COG3614  230 RMDDLLAGVLGRLAD-RDLDLRLYDGTDPGPPQLLYDSSPAAPAAaapalSATRTLEVAG--RTWTLEFRptpafeAALR 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494  533 LPIPWTAItpsILVLVITFLVGYILYEAINRIATVEEDCQkmRELKARAEAADIAKSQFLATVSHEIR 600
Cdd:COG3614  307 SWLPWLVL---LGGLLLSLLLALLLLSLARRRRRAEALAA--ARAALRALRAAELRLRALLRRALLAL 369
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
699-862 3.73e-26

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: 103.99  E-value: 3.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    699 GDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEVkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfkt 778
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGEL------------------------------------------- 37
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    779 cystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMQADSstsRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGST 858
Cdd:pfam02518   38 --------------TLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTT 100

                   ....
gi 18421494    859 FSFT 862
Cdd:pfam02518  101 VTLT 104
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
590-862 1.07e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 97.40  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   590 QFLATVSHEIRTPMNGVlgmlKMLMDT------DLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELENVPFDM 663
Cdd:NF040691  273 RFVSDVSHELRTPLTTI----RMAADVihdsrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDL 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   664 RFILDNVSSLLSGKANEKGIELAVYVSSQvPDVVVGDPSRFRQIITNLVGNSIkftqerghifisvhladevkepltied 743
Cdd:NF040691  349 RPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEVDPRRVERVLRNLVVNAI--------------------------- 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   744 avlkqrlalgcsESGEtvsGFPAVnawgswknfktcySTESQNSDQIKllVTVEDTGVGIPVDAQGRIFTPFMQADSSTS 823
Cdd:NF040691  401 ------------EHGE---GKPVV-------------VTVAQDDTAVA--VTVRDHGVGLKPGEVALVFDRFWRADPARA 450
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 18421494   824 RTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:NF040691  451 RTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
557-853 1.04e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 87.57  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   557 LYEAINRIATVEEDCQKMRElkaraeaadiaksQFLATVSHEIRTPMNGVLGMLKMLMD--TDLDAKQMDYAQTAHGSgk 634
Cdd:NF012163  222 LAQDFNQLASTLEKNEQMRR-------------DFMADISHELRTPLAVLRAELEAIQDgiRKFTPESLDSLQAEVGT-- 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   635 dLTSLINEVLDQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVpdVVVGDPSRFRQIITNLVGN 714
Cdd:NF012163  287 -LTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLEN 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   715 SIKFTQERGHIFISVhladevkepltiedavlkqrlalgcSESGETVSgfpavnawgswknfktcystesqnsdqikllV 794
Cdd:NF012163  364 SLRYTDSGGSLHISA-------------------------SQRPKEVT-------------------------------L 387
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494   795 TVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEP 853
Cdd:NF012163  388 TVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSP 446
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
578-1172 5.09e-108

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 361.09  E-value: 5.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   578 KARA-EAADIaKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLEL 656
Cdd:PRK11107  283 KKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   657 ENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTqERGHIFISVHLadevk 736
Cdd:PRK11107  362 ENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFT-ESGNIDILVEL----- 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   737 epltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystESQNSDQIKLLVTVEDTGVGIPVDAQGRIFTPFM 816
Cdd:PRK11107  436 ----------------------------------------------RALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   817 QADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTGVFGKAETNTSItklerfDLAIQEFTGLRALVID 896
Cdd:PRK11107  470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDLNPNPIID------GLPTDCLAGKRLLYVE 543
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   897 NRNIRAEVTRYELRRLGISADIVSSLrmactcciSKLENLA--MILIDKDAWNKEEFSVLDELFTRSKvtfTRVPKIFLL 974
Cdd:PRK11107  544 PNSAAAQATLDILSETPLEVTYSPTL--------SQLPEAHydILLLGLPVTFREPLTMLHERLAKAK---SMTDFLILA 612
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   975 ATSATLTERSEMKSTGlIDEVVIKPLRMSVLICCLQETlvngkkrQPNRQRRNLGHLLREKQ---ILVVDDNLVNrrvae 1051
Cdd:PRK11107  613 LPCHEQVLAEQLKQDG-ADACLSKPLSHTRLLPALLEP-------CHHKQPPLLPPTDESRLpltVMAVDDNPAN----- 679
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1052 gaLKKYGA--------IVTCvESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELerEINKkiasgevsaemfc 1123
Cdd:PRK11107  680 --LKLIGAlleeqvehVVLC-DSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELIRQL--PHNQ------------- 740
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*....
gi 18421494  1124 kfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:PRK11107  741 -----NTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRY 784
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
578-1171 5.30e-72

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: 260.10  E-value: 5.30e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    578 KARAEA--ADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLE 655
Cdd:TIGR02956  452 KARAEAeeANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLS 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    656 LENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQeRGHIFISVHLAdev 735
Cdd:TIGR02956  532 ISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTD-RGSVVLRVSLN--- 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    736 kepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsDQIKLLVTVEDTGVGIPVDAQGRIFTPF 815
Cdd:TIGR02956  608 ----------------------------------------------------DDSSLLFEVEDTGCGIAEEEQATLFDAF 635
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    816 MQADSstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTgvfgkaetntsitkLErfdlaiqeftglralvi 895
Cdd:TIGR02956  636 TQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFT--------------LP----------------- 682
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    896 dnrniraevtryelrrlgisadivsslrmactccisklenlamilidkdawnkeefsvldelFTRSKvtftrvpkifLLA 975
Cdd:TIGR02956  683 --------------------------------------------------------------LTRGK----------PAE 690
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    976 TSATLTersemkstgLIDevvIKPLRmsvlicclqetlvngkkrqpnrqrrnlghllrekqILVVDDNLVNRRVAEGALK 1055
Cdd:TIGR02956  691 DSATLT---------VID---LPPQR-----------------------------------VLLVEDNEVNQMVAQGFLT 723
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   1056 KYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELEREINKkiasgevsaemfckfsswhVPILAM 1135
Cdd:TIGR02956  724 RLGHKVTLAESGQSALECFH-QHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNE-------------------VKFIAF 783
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 18421494   1136 TADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:TIGR02956  784 SAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
575-862 6.34e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 237.50  E-value: 6.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  575 RELKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTdLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRL 654
Cdd:COG0642   97 LALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE-LDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  655 ELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADE 734
Cdd:COG0642  176 ELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGTVTVSVRREGD 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  735 vkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTP 814
Cdd:COG0642  255 --------------------------------------------------------RVRISVEDTGPGIPPEDLERIFEP 278
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18421494  815 FMQADSstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG0642  279 FFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
PRK15347 PRK15347
two component system sensor kinase;
565-1159 2.08e-68

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 248.79  E-value: 2.08e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   565 ATVEEDCQKMRELKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVL 644
Cdd:PRK15347  375 NKVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLL 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   645 DQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTqERGH 724
Cdd:PRK15347  455 DFSRIESGQMTLSLEETALLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFT-ETGG 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   725 IFISVhladevkepltiedAVLKQRLALgcsesgetvsgfpavnawgswknfktcystesqnsdqikllvTVEDTGVGIP 804
Cdd:PRK15347  534 IRLRV--------------KRHEQQLCF------------------------------------------TVEDTGCGID 557
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   805 VDAQGRIFTPFMQADSstsrTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSftgvfgkaetntsitklerFDLAI 884
Cdd:PRK15347  558 IQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFS-------------------LVLPL 614
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   885 QEFTglrALVIDNRNIRAEVTRY-ELRRLGISadivsslrmactcCISKLENLAmiLIDKDawnkeefsvldelftrskv 963
Cdd:PRK15347  615 NEYA---PPEPLKGELSAPLALHrQLSAWGIT-------------CQPGHQNPA--LLDPE------------------- 657
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   964 tftrvpkifLLATSATLTERsemkstglidevvikplrmsvliccLQETLVNgkkrQPNRQRRNLGHLLREKQILVVDDN 1043
Cdd:PRK15347  658 ---------LAYLPGRLYDL-------------------------LQQIIQG----APNEPVINLPLQPWQLQILLVDDV 699
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1044 LVNRRVAEGALKKYGAIVTCVESGKAALAmLKPPHNFDACFMDLQMPEMDGFEATRRVRELEREINKkiasgevsaemfc 1123
Cdd:PRK15347  700 ETNRDIIGMMLVELGQQVTTAASGTEALE-LGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPNNLDP------------- 765
                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 18421494  1124 kfsswHVPILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:PRK15347  766 -----DCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
573-862 1.85e-62

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 212.84  E-value: 1.85e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  573 KMRELKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMD--TDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIE 650
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDeeDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  651 SGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVH 730
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGGTITISAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  731 LADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGR 810
Cdd:COG2205  160 REGD--------------------------------------------------------GVRISVSDNGPGIPEEELER 183
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18421494  811 IFTPFMQADSstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG2205  184 IFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
580-862 8.82e-62

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 216.34  E-value: 8.82e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  580 RAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMD--TDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELE 657
Cdd:COG5002  157 ELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLE 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  658 NVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEvke 737
Cdd:COG5002  237 KEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREEDD--- 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  738 pltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPFMQ 817
Cdd:COG5002  313 -----------------------------------------------------QVRISVRDTGIGIPEEDLPRIFERFYR 339
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 18421494  818 ADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG5002  340 VDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTIT 384
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
563-944 3.72e-48

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 186.65  E-value: 3.72e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   563 RIATVEEDCQKMRELKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINE 642
Cdd:PRK11466  419 RTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILND 498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   643 VLDQAKIESG--RLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTq 720
Cdd:PRK11466  499 ILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFT- 577
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   721 ERGHIfisvhladevkepltiedavlkqRLALGCSESgetvsgfpavnawgSWknfktcystesqnsdqiklLVTVEDTG 800
Cdd:PRK11466  578 DEGSI-----------------------VLRSRTDGE--------------QW-------------------LVEVEDSG 601
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   801 VGIPVDAQGRIFTPFMQAdsstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTGVFGKAETNTSITKLERF 880
Cdd:PRK11466  602 CGIDPAKLAEIFQPFVQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPVPKTVNQAV 677
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494   881 DLaiqefTGLRALVIDNRNIRAEVTRYELRRLGISADIVSSLRMACTcCISKLENLAMILIDKD 944
Cdd:PRK11466  678 RL-----DGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALE-TLQNSEPFAAALVDFD 735
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
576-1175 4.02e-48

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 185.14  E-value: 4.02e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   576 ELKARAEAADIA---KSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESG 652
Cdd:PRK11091  268 ERKRYQDALEKAsrdKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERR 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   653 RLELENVPFDMR-FI--LDNVSSLLsgkANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQErGHIFISV 729
Cdd:PRK11091  348 KLQLDNQPIDFTdFLadLENLSGLQ---AEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQ-GGVTVRV 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   730 hlADEVKEPLTIEdavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqikllvtVEDTGVGIPVDAQG 809
Cdd:PRK11091  424 --RYEEGDMLTFE-----------------------------------------------------VEDSGIGIPEDELD 448
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   810 RIFTPFMQA-DSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFTgvfgkaetntsitklerfdlaiqeft 888
Cdd:PRK11091  449 KIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLT-------------------------- 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   889 glralvidnrniraevtryelrrlgISADIVsslrmactccisklenlamilidkdAWNKEEFSVLDELftrskvtftrv 968
Cdd:PRK11091  503 -------------------------IHAPAV-------------------------AEEVEDAFDEDDM----------- 521
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   969 pkifllatsatltersemkstglidevvikplrmsvlicclqetlvngkkrqpnrqrrnlghLLREKQILVVDDNLVNRR 1048
Cdd:PRK11091  522 --------------------------------------------------------------PLPALNILLVEDIELNVI 539
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1049 VAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRelEREINKKIAsgevsaemfckfssw 1128
Cdd:PRK11091  540 VARSVLEKLGNSVDVAMTGKEALEMFD-PDEYDLVLLDIQLPDMTGLDIARELR--ERYPREDLP--------------- 601
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 18421494  1129 hvPILAMTADVIQAThEECMKCGMDGYVSKPFEEEVLYTAVARFFEP 1175
Cdd:PRK11091  602 --PLVALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKKFWDT 645
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
704-862 1.88e-47

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: 164.59  E-value: 1.88e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  704 FRQIITNLVGNSIKFTqERGHIFISVHLadevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystE 783
Cdd:cd16922    1 LRQILLNLLGNAIKFT-EEGEVTLRVSL---------------------------------------------------E 28
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  784 SQNSDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16922   29 EEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQGSTFTFT 107
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
568-1170 1.57e-45

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 178.24  E-value: 1.57e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   568 EEDCQKMrelKARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQA 647
Cdd:PRK10841  430 EESLQEM---AQAAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFS 506
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   648 KIESGRLELENVPFD----MRFILDNVSSLLSGKAnekgIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTqERG 723
Cdd:PRK10841  507 KIESEQLKIEPREFSprevINHITANYLPLVVKKR----LGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFT-DTG 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   724 HIFISVHLADevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktCYstesqnsdqikLLVTVEDTGVGI 803
Cdd:PRK10841  582 CIVLHVRVDG---------------------------------------------DY-----------LSFRVRDTGVGI 605
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   804 PVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSF---------------TGVFGK- 867
Cdd:PRK10841  606 PAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIriplygaqypqkkgvEGLQGKr 685
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   868 ---AETNTSitkLERFDLAIQEFTGLRALVIDNRNIRAE---VTRYELrrlgisaDIVSSLRmactccisklenlAMILI 941
Cdd:PRK10841  686 cwlAVRNAS---LEQFLETLLQRSGIQVQRYEGQEPTPEdvlITDDPV-------QKKWQGR-------------AVITF 742
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   942 DkdawnKEEFSVLDElftrskvtftRVPKIFLLATsATLTErsemkstglIDEVVIKPLRMSVLICCLQETLVngkkrQP 1021
Cdd:PRK10841  743 C-----RRHIGIPLE----------IAPGEWVHST-ATPHE---------LPALLARIYRIELESDDSANALP-----ST 792
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1022 NRQRRNLGHLLrekqILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHnFDACFMDLQMPEMDGFEATRRV 1101
Cdd:PRK10841  793 DKAVSDNDDMM----ILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNH-IDIVLTDVNMPNMDGYRLTQRL 867
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  1102 RELEREInkkiasgevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVA 1170
Cdd:PRK10841  868 RQLGLTL----------------------PVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLT 914
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
1037-1169 2.63e-44

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: 155.71  E-value: 2.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasge 1116
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE-EPFDLVLMDLQMPVMDGLEATRRIRELEG---------- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1117 vsaemfckfSSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17546   70 ---------GGRRTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
304-499 3.52e-43

CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 427591  Cd Length: 184  Bit Score: 155.53  E-value: 3.52e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    304 SAIDQRTFEEYTERTNFERPLTSGVAYALKVPHSEREKFEKEH------GWAIKkmetedqtvvqdcvpenfdPAPIQDE 377
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR-------------------PAGDRDE 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    378 YAPVIFAQETVSH--IVSVDMMSGEEDRENILRARASGKGVLTSPFKLL--KSNHLGVVLTFAVYDTSLPPdaTEEQRVE 453
Cdd:pfam03924   62 YFPIIYIEPLAGNnrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRA 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 18421494    454 ATIGYLGASYDMPSLVEKLLHQLASkQTIAVDVYDTTNTSGLIKMY 499
Cdd:pfam03924  140 ALLGFVYAPFRIDDLLEAALLRLGE-DGLDLALYDGTSASAPELLY 184
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
535-862 8.05e-42

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 161.49  E-value: 8.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  535 IPWTAITPSILVLVITFLVGYILYEAINRIATVEEDCQKMRELKARA---EAADIAKSQFLATVSHEIRTPMNGVLGMLK 611
Cdd:COG4251  226 GLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTaelERSNEELEQFAYVASHDLREPLRKISGFSQ 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  612 ML---MDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIesGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVy 688
Cdd:COG4251  306 LLeedYGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEV- 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  689 vsSQVPdVVVGDPSRFRQIITNLVGNSIKFTQERghifisvhladevkEPLTIEdavlkqrlaLGCSESGETVsgfpavn 768
Cdd:COG4251  383 --GPLP-TVRGDPTLLRQVFQNLISNAIKYSRPG--------------EPPRIE---------IGAEREGGEW------- 429
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  769 awgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSrtYGGTGIGLSISKRLVELMQGEMG 848
Cdd:COG4251  430 ------------------------VFSVRDNGIGIDPEYAEKIFEIFQRLHSRDE--YEGTGIGLAIVKKIVERHGGRIW 483
                        330
                 ....*....|....
gi 18421494  849 FVSEPGIGSTFSFT 862
Cdd:COG4251  484 VESEPGEGATFYFT 497
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
573-862 7.60e-38

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: 148.97  E-value: 7.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  573 KMRELKARAEAADIAkSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMdYAQTAHGSGKDLTSLINEVLDQAKIESG 652
Cdd:COG5809  256 KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKT-YLDIMLSELDRIESIISEFLVLAKPQAI 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  653 RLElenvPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDvVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLA 732
Cdd:COG5809  334 KYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEGGNITIETKAE 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  733 DEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsDQIklLVTVEDTGVGIPVDAQGRIF 812
Cdd:COG5809  409 DD-----------------------------------------------------DKV--VISVTDEGCGIPEERLKKLG 433
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18421494  813 TPFMqadsstSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG5809  434 EPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
1032-1174 1.20e-37

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: 137.29  E-value: 1.20e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1032 LREKQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkk 1111
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA-GPPDLILLDINMPGMDGLELLRRIRALPR----- 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1112 iasgevsaemfckfsSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:COG0784   77 ---------------LPDIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLA 124
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
591-862 6.85e-33

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: 130.79  E-value: 6.85e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    591 FLATVSHEIRTPMNGVLGMLKMLMDT--DLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELENVPFDMRFILD 668
Cdd:TIGR02966  117 FVANVSHELRTPLTVLRGYLETLADGpdEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLD 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    669 NVSSLLSGKANEKGIELAVYVSSQVPdvVVGDPSRFRQIITNLVGNSIKFTQERGHIfisvhladevkepltiedavlkq 748
Cdd:TIGR02966  197 HLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTPEGGTI----------------------- 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    749 rlalgcsesgeTVsgfpavnawgSWKnfktcystesqnSDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGG 828
Cdd:TIGR02966  252 -----------TV----------RWR------------RDGGGAEFSVTDTGIGIAPEHLPRLTERFYRVDKSRSRDTGG 298
                          250       260       270
                   ....*....|....*....|....*....|....
gi 18421494    829 TGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:TIGR02966  299 TGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
1037-1172 4.37e-32

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: 123.48  E-value: 4.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasge 1116
Cdd:COG3706    4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQE-HRPDLILLDLEMPDMDGLELCRRLRADPRTA-------- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1117 vsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAV---ARF 1172
Cdd:COG3706   75 ------------DIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARVdlvARY 121
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
569-1005 9.07e-32

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 134.86  E-value: 9.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   569 EDCQKMREL-------KARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQ-MDYAQTAHGSGKDLTSLI 640
Cdd:PRK09959  686 QDITETRDLihaleveRNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQrVEAISLAYATGQSLLGLI 765
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   641 NEVLDQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAvyVSSQVPD--VVVGDPSRFRQIITNLVGNSIKF 718
Cdd:PRK09959  766 GEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALS--CSSTFPDhyLVKIDPQAFKQVLSNLLSNALKF 843
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   719 TQErGHIFISVHLadevkepLTIEDavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqNSDQIKLlvTVED 798
Cdd:PRK09959  844 TTE-GAVKITTSL-------GHIDD------------------------------------------NHAVIKM--TIMD 871
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   799 TGVGIPVDAQGRIFTPFMQadSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT----------GVFGKA 868
Cdd:PRK09959  872 SGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITipveisqqvaTVEAKA 949
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   869 EtnTSITKLERfdlaiqeftgLRALVIDNRNIRAEVTRYELRRLGISADIVSSLRMACTCCisKLENLAMILIDKDAWNK 948
Cdd:PRK09959  950 E--QPITLPEK----------LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKV--SMQHYDLLITDVNMPNM 1015
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494   949 EEFsvldELFTRSKVTFTRVPkIFLLATSATLTERSEMKSTGLiDEVVIKPLRMSVL 1005
Cdd:PRK09959 1016 DGF----ELTRKLREQNSSLP-IWGLTANAQANEREKGLSCGM-NLCLFKPLTLDVL 1066
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
528-862 9.60e-31

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 125.30  E-value: 9.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  528 RFKHKLPIPWTAITPSILVLVITFLVGYILYEAINRIATVEEDCQKMRELKARAEAADIAKSQFL------------ATV 595
Cdd:COG4191   70 ALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVqseklaalgelaAGI 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  596 SHEIRTPMNGVLG---MLKMLMDTDLDAKQM-DYAQTAHGSGKDLTSLINEVLDQAKIESGRLElenvPFDMRFILDNVS 671
Cdd:COG4191  150 AHEINNPLAAILGnaeLLRRRLEDEPDPEELrEALERILEGAERAAEIVRSLRAFSRRDEEERE----PVDLNELIDEAL 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  672 SLLSGKANEKGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIkftqerghifisvhladevkepltieDAVLKQ--- 748
Cdd:COG4191  226 ELLRPRLKARGIEVELDLPPDLP-PVLGDPGQLEQVLLNLLINAI--------------------------DAMEEGegg 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  749 RLALGCSESGETVsgfpavnawgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMqadsSTSRTYGG 828
Cdd:COG4191  279 RITISTRREGDYV-------------------------------VISVRDNGPGIPPEVLERIFEPFF----TTKPVGKG 323
                        330       340       350
                 ....*....|....*....|....*....|....
gi 18421494  829 TGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG4191  324 TGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
699-862 2.85e-30

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 115.82  E-value: 2.85e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     699 GDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfkt 778
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGD-------------------------------------------- 36
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     779 cystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPFMQADSsTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGST 858
Cdd:smart00387   37 ------------HVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISVESEPGGGTT 103

                    ....
gi 18421494     859 FSFT 862
Cdd:smart00387  104 FTIT 107
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
304-488 5.77e-30

This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.


Pssm-ID: 215015  Cd Length: 176  Bit Score: 117.44  E-value: 5.77e-30
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     304 SAIDQRTFEEYTERTNFER--PLTSGVAYALKVPHSEREKFEkehgWAIKKMETEDQTVVQDcvpenfdPAPIQDEYAPV 381
Cdd:smart01079    2 ESVSRAEFRRFALELQLNRrlPGIQGLGWAPRVPPAERAAFE----AALRAGGPGLFNIRLA-------PDGERDEYFVI 70
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494     382 IFAQETVSH--IVSVDMMSGEEDRENILRARASGKGVLTSPFKLLKSNH--LGVVLTFAVYDtslpPDATEEQRVEATIG 457
Cdd:smart01079   71 TYIEPLAGNeaALGLDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGdgRGFLLRLPVYR----GGPPTSTRREALWG 146
                           170       180       190
                    ....*....|....*....|....*....|.
gi 18421494     458 YLGASYDMPSLVEKLLHQLASKQtIAVDVYD 488
Cdd:smart01079  147 FVSAVFRLDDLLEGLLGALDLPG-LDLALYD 176
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
549-862 6.30e-30

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


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 123.92  E-value: 6.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  549 ITFLVGYILYEAINRIATVEEdcqkMRELKARAEAAdiAKSQFLATVSHEIR---TPMNGVLGMLKMLMD---TDLDAKQ 622
Cdd:COG5000  168 RTLLVRASPLRDDGYVIVFDD----ITELLRAERLA--AWGELARRIAHEIKnplTPIQLSAERLRRKLAdklEEDREDL 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  623 MDYAQTAHGSGKDLTSLINEVLDQAKIESGRLElenvPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdVVVGDPS 702
Cdd:COG5000  242 ERALDTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLP-EVLADRD 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  703 RFRQIITNLVGNSIKFTQERGHIFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcyst 782
Cdd:COG5000  317 QLEQVLINLLKNAIEAIEEGGEIEVSTRREDG------------------------------------------------ 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  783 esqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTyGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG5000  349 --------RVRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
572-860 4.60e-29

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 120.34  E-value: 4.60e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  572 QKMRELKARAEAAdiakSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIES 651
Cdd:COG3852  123 ERELRRAEKLAAV----GELAAGLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRP 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  652 GRLElenvPFDMRFILDNVSSLLSGKANeKGIELAVYVSSQVPDVVvGDPSRFRQIITNLVGNSIKFTQERGHIFISVhl 731
Cdd:COG3852  199 PERE----PVNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPEVL-GDPDQLIQVLLNLVRNAAEAMPEGGTITIRT-- 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  732 adevkepltiedavlkqRLALGCSESGETVSGFpavnawgswknfktcystesqnsdqikLLVTVEDTGVGIPVDAQGRI 811
Cdd:COG3852  271 -----------------RVERQVTLGGLRPRLY---------------------------VRIEVIDNGPGIPEEILDRI 306
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 18421494  812 FTPFMqadssTSRTyGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFS 860
Cdd:COG3852  307 FEPFF-----TTKE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFR 349
CHASE1 COG3614
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
234-600 2.05e-27

Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442832 [Multi-domain]  Cd Length: 588  Bit Score: 119.02  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  234 ILLLGILggVSFSVWWF-WDTNEEIIMKRRETLAnmcDERARVLQDQFNvslNHVHALSILVSTFHHgkiPSAIDQRTFE 312
Cdd:COG3614   17 VLLLGLL--LTALAWWAvRRAEEQRARARFERLA---DELASALEERLD---AYEQVLRGLAGLFAA---SDDVTRAEFR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  313 EYTERTNFERPLTS--GVAYALKVPHSEREKFEkehgwaikkmetedQTVVQDCVPeNFD--PAPIQDEYAPVIF---AQ 385
Cdd:COG3614   86 RYVASLDLLRRYPGiqGLGWAPRVPAAERAAFE--------------AAARAEGFP-DFRirPAGERDEYFPITYiepLD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  386 ETVSHIVSVDMMSGEEDRENILRARASGKGVLTSPFKLL--KSNHLGVVLTFAVYDTSLPPDaTEEQRVEATIGYLGASY 463
Cdd:COG3614  151 ARNRRALGFDMASEPVRRAAMERARDTGRPAASGPVTLVqeTDGQPGFLLYLPVYRGGAPPD-TVAERRAALRGFVYAPF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  464 DMPSLVEKLLHQLASkQTIAVDVYDTTNTSGLIKMYGSEIGDISE-----QHISSLDFGDpsRNHEMHCR------FKHK 532
Cdd:COG3614  230 RMDDLLAGVLGRLAD-RDLDLRLYDGTDPGPPQLLYDSSPAAPAAaapalSATRTLEVAG--RTWTLEFRptpafeAALR 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494  533 LPIPWTAItpsILVLVITFLVGYILYEAINRIATVEEDCQkmRELKARAEAADIAKSQFLATVSHEIR 600
Cdd:COG3614  307 SWLPWLVL---LGGLLLSLLLALLLLSLARRRRRAEALAA--ARAALRALRAAELRLRALLRRALLAL 369
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
699-862 3.73e-26

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: 103.99  E-value: 3.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    699 GDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEVkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfkt 778
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEITVTLSEGGEL------------------------------------------- 37
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    779 cystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMQADSstsRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGST 858
Cdd:pfam02518   38 --------------TLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSIVRKLVELLGGTITVESEPGGGTT 100

                   ....
gi 18421494    859 FSFT 862
Cdd:pfam02518  101 VTLT 104
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
1037-1170 1.12e-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: 102.61  E-value: 1.12e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasge 1116
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKE-ERPDLILLDINMPGMDGLELLKRIRRRDP---------- 69
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 18421494   1117 vsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVA 1170
Cdd:pfam00072   70 ------------TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
1035-1171 4.34e-25

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 104.27  E-value: 4.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkias 1114
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEE-ERPDLILLDLMLPGMDGLEVCRRLRARPS-------- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1115 gevsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:COG0745   73 --------------DIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL---LAR 112
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
1037-1174 2.29e-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: 102.94  E-value: 2.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasge 1116
Cdd:COG3437    9 VLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLE-APPDLILLDVRMPGMDGFELLRLLRADPSTR-------- 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1117 vsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:COG3437   80 ------------DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRNALE 125
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
1038-1159 1.26e-23

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: 96.14  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1038 LVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasgev 1117
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE-ERPDLVLLDLMMPGMDGLELLRKLRELPP----------- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18421494 1118 saemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:cd00156   69 -----------DIPVIVLTAKADEEDAVRALELGADDYLVKP 99
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
1036-1159 1.85e-22

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: 93.62  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1036 QILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKP-PHNFDACFMDLQMPEMDGFEATRRVRElereinkkias 1114
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASaEHSFQLVLLDLCMPEMDGFEVALRIRK----------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18421494 1115 gevsaemFCKFSSWHVpILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:cd19933   71 -------LFGRRERPL-IVALTANTDDSTREKCLSLGMNGVITKP 107
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
1033-1174 4.02e-22

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: 100.42  E-value: 4.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1033 REKQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELEREInkki 1112
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLR-EEPPDLVLLDLRMPGMDGLELLRELRALDPDL---- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1113 asgevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:COG2204   76 ------------------PVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALE 119
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
543-854 1.04e-20

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: 96.69  E-value: 1.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    543 SILVLVITFLVGYI-----------LYEAINRIaTVEEDCQKMRELKARAEAADIAK----------------SQFLATV 595
Cdd:TIGR01386  170 AVLLVLLTALLGWWitrlgleplrrLSAVAARI-SPESLDQRLDPSRAPAELRELAQsfnamlgrledafqrlSQFSADL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    596 SHEIRTPMNGVLGMLKMLMDTDLDAKqmDYAQTAHGSGKD---LTSLINEVLDQAKIESGRLELENVPFDMRFILDNVSS 672
Cdd:TIGR01386  249 AHELRTPLTNLLGQTQVALSQPRTGE--EYREVLESNLEElerLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVAE 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    673 LLSGKANEKGIELAVYVSSQVPdvvvGDPSRFRQIITNLVGNSIKFTQERGHifISVHLADevkepltiedavlkqrlal 752
Cdd:TIGR01386  327 YFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGT--ITVRIER------------------- 381
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    753 gcsESGETvsgfpavnawgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIG 832
Cdd:TIGR01386  382 ---RSDEV--------------------------------RVSVSNPGPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLG 426
                          330       340
                   ....*....|....*....|..
gi 18421494    833 LSISKRLVELMQGEMGFVSEPG 854
Cdd:TIGR01386  427 LAIVRSIMEAHGGRASAESPDG 448
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
590-862 1.07e-20

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 97.40  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   590 QFLATVSHEIRTPMNGVlgmlKMLMDT------DLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELENVPFDM 663
Cdd:NF040691  273 RFVSDVSHELRTPLTTI----RMAADVihdsrdDFDPATARSAELLHTELDRFESLLSDLLEISRFDAGAAELDVEPVDL 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   664 RFILDNVSSLLSGKANEKGIELAVYVSSQvPDVVVGDPSRFRQIITNLVGNSIkftqerghifisvhladevkepltied 743
Cdd:NF040691  349 RPLVRRVVDALRQLAERAGVELRVDAPGT-PVVAEVDPRRVERVLRNLVVNAI--------------------------- 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   744 avlkqrlalgcsESGEtvsGFPAVnawgswknfktcySTESQNSDQIKllVTVEDTGVGIPVDAQGRIFTPFMQADSSTS 823
Cdd:NF040691  401 ------------EHGE---GKPVV-------------VTVAQDDTAVA--VTVRDHGVGLKPGEVALVFDRFWRADPARA 450
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 18421494   824 RTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:NF040691  451 RTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
1037-1171 5.43e-20

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 86.44  E-value: 5.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereiNKKIAsge 1116
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARK-EKPDLILMDIQLPGMDGLEATRLLKE-----DPATR--- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494 1117 vsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:cd17548   73 ------------DIPVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
587-652 3.79e-19

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 82.23  E-value: 3.79e-19
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494     587 AKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESG 652
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
587-652 6.34e-19

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 81.87  E-value: 6.34e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494    587 AKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESG 652
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
PRK09303 PRK09303
histidine kinase;
587-862 3.12e-18

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 88.08  E-value: 3.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   587 AKSQFLATVSHEIRTPMNGV---LGMLKMLMDTDLDAKQMDYAQ----TAHGSGKDLTSLINEVLDQAKIESGRLELENV 659
Cdd:PRK09303  150 FKDRVLAMLAHDLRTPLTAAslaLETLELGQIDEDTELKPALIEqlqdQARRQLEEIERLITDLLEVGRTRWEALRFNPQ 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   660 PFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVvGDPSRFRQIITNLVGNSIKFTQERGHIFISV-Hladevkep 738
Cdd:PRK09303  230 KLDLGSLCQEVILELEKRWLAKSLEIQTDIPSDLPSVY-ADQERIRQVLLNLLDNAIKYTPEGGTITLSMlH-------- 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   739 ltiedavlkqrlalgcsesgetvsgfpavnawgswknfKTcysteSQnsdqiKLLVTVEDTGVGIPVDAQGRIF--TPFM 816
Cdd:PRK09303  301 --------------------------------------RT-----TQ-----KVQVSICDTGPGIPEEEQERIFedRVRL 332
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 18421494   817 QADSSTSrtygGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:PRK09303  333 PRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFT 374
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
557-853 1.04e-17

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 87.57  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   557 LYEAINRIATVEEDCQKMRElkaraeaadiaksQFLATVSHEIRTPMNGVLGMLKMLMD--TDLDAKQMDYAQTAHGSgk 634
Cdd:NF012163  222 LAQDFNQLASTLEKNEQMRR-------------DFMADISHELRTPLAVLRAELEAIQDgiRKFTPESLDSLQAEVGT-- 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   635 dLTSLINEVLDQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVpdVVVGDPSRFRQIITNLVGN 714
Cdd:NF012163  287 -LTKLVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLEN 363
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   715 SIKFTQERGHIFISVhladevkepltiedavlkqrlalgcSESGETVSgfpavnawgswknfktcystesqnsdqikllV 794
Cdd:NF012163  364 SLRYTDSGGSLHISA-------------------------SQRPKEVT-------------------------------L 387
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494   795 TVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEP 853
Cdd:NF012163  388 TVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSP 446
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
567-862 1.10e-17

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 86.99  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   567 VEEDCQKMRELKAraeaadiAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYA-QTAHGSGKDLTSLINEVLD 645
Cdd:PRK11006  190 VARDVTQMHQLEG-------ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKAlHTMREQTQRMEGLVKQLLT 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   646 QAKIESG-RLELE---NVPfDMRFILDNVSSLLSGKANekgiELAVYVSSQVPdvVVGDPSRFRQIITNLVGNSIKFTQE 721
Cdd:PRK11006  263 LSKIEAApTIDLNekvDVP-MMLRVLEREAQTLSQGKH----TITFEVDNSLK--VFGNEDQLRSAISNLVYNAVNHTPE 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   722 RGHIFISvhladevkepltiedavlkqrlalgcsesgetvsgfpavnaWgswknfktcystesQNSDQIKLLvTVEDTGV 801
Cdd:PRK11006  336 GTHITVR-----------------------------------------W--------------QRVPQGAEF-SVEDNGP 359
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494   802 GIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:PRK11006  360 GIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFV 420
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
1037-1169 1.15e-17

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: 79.81  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLkPPHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasGE 1116
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA-QRFRPDVILSDIGMPGMDGYELARRLRELPW--------LA 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1117 vsaemfckfsswHVPILAMTA-----DVIQATHEecmkcGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17580   72 ------------NTPAIALTGygqpeDRERALEA-----GFDAHLVKPVDPDELIELI 112
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
1037-1160 3.08e-17

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: 78.31  E-value: 3.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasge 1116
Cdd:cd17538    2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAE-EELPDLILLDVMMPGMDGFEVCRRLKEDPE---------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18421494 1117 vsaemfckfsSWHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPF 1160
Cdd:cd17538   71 ----------TRHIPVIMITAlddreDRIRG-----LEAGADDFLSKPI 104
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
1037-1174 1.31e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 77.70  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYG--AIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkias 1114
Cdd:COG4565    6 VLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAE-HRPDLILLDIYLPDGDGLELLRELRARGP-------- 76
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1115 gevsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:COG4565   77 --------------DVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERYLE 122
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
573-861 1.33e-16

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 85.02  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   573 KMRELKARAEA-ADIAKsqFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIEs 651
Cdd:PRK11360  376 RLQRRVARQERlAALGE--LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPR- 452
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   652 grlELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVVgDPSRFRQIITNLVGNSIKFTQERGHIFISvhl 731
Cdd:PRK11360  453 ---ESQWQPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQAISARGKIRIR--- 525
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   732 adevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcysTESQNSDQIklLVTVEDTGVGIPVDAQGRI 811
Cdd:PRK11360  526 --------------------------------------------------TWQYSDGQV--AVSIEDNGCGIDPELLKKI 553
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 18421494   812 FTPFMqadsSTSRTygGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSF 861
Cdd:PRK11360  554 FDPFF----TTKAK--GTGLGLALSQRIINAHGGDIEVESEPGVGTTFTL 597
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
1037-1159 7.89e-16

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: 74.04  E-value: 7.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVE--SGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkias 1114
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEAGFEVVGEaeNGEEALELLEE-HKPDLVITDINMPGMDGLELLEAIRELDPDT------ 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18421494 1115 gevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:COG4753   75 ----------------KIIILSGYSDFEYAQEAIKLGADDYLLKP 103
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
1035-1171 1.15e-15

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: 74.45  E-value: 1.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRELEREInkki 1112
Cdd:COG5803    3 KKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVKelKP---DLVLLDMKMPGMDGIEILKEIKEIDPDI---- 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1113 asgevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:COG5803   76 ------------------PVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNK 116
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
576-862 4.19e-15

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: 79.39  E-value: 4.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  576 ELKARAEAADIAkSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDakQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLE 655
Cdd:COG5805  276 ELMARSEKLSIA-GQLAAGIAHEIRNPLTSIKGFLQLLQPGIED--KEEYFDIMLSELDRIESIISEFLALAKPQAVNKE 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  656 LENVpfdmRFILDNVSSLLSGKANEKGIELAVYVSSQVPDVVvGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEv 735
Cdd:COG5805  353 KENI----NELIQDVVTLLETEAILHNIQIRLELLDEDPFIY-CDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDN- 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  736 kepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPF 815
Cdd:COG5805  427 -------------------------------------------------------SVIIRVIDEGIGIPEERLKKLGEPF 451
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 18421494  816 MqadsSTSRTygGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG5805  452 F----TTKEK--GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTIT 492
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
787-862 1.05e-14

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 70.89  E-value: 1.05e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494  787 SDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSStsrtygGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16920   33 ADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGLSICRSIIEAHGGRLSVESPAGGGATFQFT 102
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
1038-1159 2.88e-14

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 69.74  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1038 LVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasgev 1117
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE-EQPDLIILDVMLPGMDGFEVCRRLREKGSDI--------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18421494 1118 saemfckfsswhvPILAMTA-----DVIQAtheecMKCGMDGYVSKP 1159
Cdd:cd17574   71 -------------PIIMLTAkdeeeDKVLG-----LELGADDYITKP 99
PRK10604 PRK10604
sensor protein RstB; Provisional
588-861 3.72e-14

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 76.18  E-value: 3.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   588 KSQFLATVSHEIRTPMNGV---LGMLKMLMDTDLDAKQMDYAQtahgsgkdLTSLINEVLDQAKIESGRLELENVPFDM- 663
Cdd:PRK10604  212 KKQLIDGIAHELRTPLVRLryrLEMSDNLSAAESQALNRDIGQ--------LEALIEELLTYARLDRPQNELHLSEPDLp 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   664 ---RFILDNVSSLlsgkANEKGIELAVyvsSQVPDVVVGDPSRFRQIITNLVGNSIKFTQerghifisvhladevkeplt 740
Cdd:PRK10604  284 awlSTHLADIQAV----TPEKTVRLDT---PHQGDYGALDMRLMERVLDNLLNNALRYAH-------------------- 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   741 iedavlkQRLALGCSESGETVsgfpavnawgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMQADS 820
Cdd:PRK10604  337 -------SRVRVSLLLDGNQA-------------------------------CLIVEDDGPGIPPEERERVFEPFVRLDP 378
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 18421494   821 STSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSF 861
Cdd:PRK10604  379 SRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
587-648 4.84e-14

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: 67.62  E-value: 4.84e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494  587 AKSQFLATVSHEIRTPMNGVLGMLKMLMDTDL-DAKQMDYAQTAHGSGKDLTSLINEVLDQAK 648
Cdd:cd00082    3 AKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLSR 65
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
1036-1165 5.02e-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: 69.39  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1036 QILVVDDNLVNRRVAEGALKK--YGAIVTCVESgKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEreinkkia 1113
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSagYLEVVSFTDP-REALAWCRE-NPPDLILLDYMMPGMDGLEFIRRLRALP-------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1114 SGEvsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFE-EEVL 1165
Cdd:cd17551   72 GLE------------DVPIVMITADTDREVRLRALEAGATDFLTKPFDpVELL 112
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
705-862 6.74e-14

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: 68.89  E-value: 6.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  705 RQIITNLVGNSIKFTQERGHIFISVHlADEVKEPLTIEdavlkqrlalgcsesgetvsgfpavnawgswknfktcystes 784
Cdd:cd16921    2 GQVLTNLLGNAIKFRRPRRPPRIEVG-AEDVGEEWTFY------------------------------------------ 38
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494  785 qnsdqikllvtVEDTGVGIPVDAQGRIFTPFMQADSSTSrtYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16921   39 -----------VRDNGIGIDPEYAEKVFGIFQRLHSREE--YEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFT 103
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
700-859 8.70e-14

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: 68.67  E-value: 8.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  700 DPSRFRQIITNLVGNSIKFTQERGHIFISVHLadevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktc 779
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEK------------------------------------------------ 32
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  780 ystesqnSDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTF 859
Cdd:cd16925   33 -------FRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALF 105
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
1037-1160 9.53e-14

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


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 68.31  E-value: 9.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRvrelereinkkIAS 1114
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQaePP---DLILLDVMMPGMDGFEVCRR-----------LKA 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1115 GEVSAemfckfsswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPF 1160
Cdd:cd19920   67 DPATR---------HIPVIFLTAltdteDKVKG-----FELGAVDYITKPF 103
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-859 9.77e-14

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: 68.22  E-value: 9.77e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494  784 SQNSDQikLLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTYG-GTGIGLSISKRLVELMQGEMGFVSEPGIGSTF 859
Cdd:cd16943   30 WAHVDQ--VLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
693-860 1.10e-13

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: 69.02  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  693 VPDVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLadevkepltiedavlkqrlalgcsesgETVSGFPAVNAWGS 772
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGGGNITFRVFL---------------------------EGGSEDRSDRDWGP 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  773 WKnfktcySTESQNSDQIKLLVTVEDTGvgipvdaQGRIFTPFMQAdsSTSRTYG----GTGIGLSISKRLVELMQGEMG 848
Cdd:cd16938   54 WR------PSMSDESVEIRFEVEINDSG-------SPSIESASMRN--SLNRRYNlselGEHLSFSICKQLVQLMGGNIW 118
                        170
                 ....*....|..
gi 18421494  849 FVSEPGIGSTFS 860
Cdd:cd16938  119 IVPGSGLGTTMS 130
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
528-859 1.16e-13

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 75.87  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   528 RFKHKLPIPWTAItpSILVLVITFLVGYIlyeainRIATVEEDCqkmRELKARAEAAdiaksQFLATV-------SHEIR 600
Cdd:PRK13837  399 RQRYGLRPPAGEL--QLLELALDCLAHAI------ERRRLETER---DALERRLEHA-----RRLEAVgtlasgiAHNFN 462
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   601 TPMNGVLGMLKMLMDT-DLDAKQMDYAQTAHGSGKDLTSLINEVLDQakieSGRLELENVPFDMRFILDNVSSLLSGkAN 679
Cdd:PRK13837  463 NILGAILGYAEMALNKlARHSRAARYIDEIISAGARARLIIDQILAF----GRKGERNTKPFDLSELVTEIAPLLRV-SL 537
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   680 EKGIELAVYvSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEVKepltiedavlKQRLALGCSESGE 759
Cdd:PRK13837  538 PPGVELDFD-QDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGRVDISLSRAKLRA----------PKVLSHGVLPPGR 606
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   760 TVsgfpavnawgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTyGGTGIGLSISKRL 839
Cdd:PRK13837  607 YV-------------------------------LLRVSDTGAGIDEAVLPHIFEPFF-----TTRA-GGTGLGLATVHGI 649
                         330       340
                  ....*....|....*....|
gi 18421494   840 VELMQGEMGFVSEPGIGSTF 859
Cdd:PRK13837  650 VSAHAGYIDVQSTVGRGTRF 669
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
1037-1165 1.36e-13

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: 68.52  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAMLKPPhNFDACFMDLQMPEMDGFEATRRVRelereinkkiASG 1115
Cdd:cd19923    3 VLVVDDFSTMRRIIKNLLKELGfNNVEEAEDGVDALEKLKAG-GFDFVITDWNMPNMDGLELLKTIR----------ADG 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494 1116 EVSaemfckfsswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVL 1165
Cdd:cd19923   72 ALS----------HLPVLMVTAeakkeNVIAA-----AQAGVNNYIVKPFTAATL 111
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
1035-1172 1.41e-13

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: 68.48  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPhNFDACFMDLQMPEMDGFEATRRVRELereinkkias 1114
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSK-KFDLIITDQNMPNMDGIELIKELRKL---------- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1115 gevSAEMFckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:cd17562   70 ---PAYKF-------TPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKV 117
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
1033-1174 1.53e-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: 70.37  E-value: 1.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1033 REKQILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkk 1111
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGyEVVAEAADGEDAVELVRE-LKPDLVIVDIDMPDRDGLEAARQISEERP----- 75
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1112 iasgevsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYT----AVARFFE 1174
Cdd:COG3707   76 ------------------APVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPalelALARFRE 124
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
562-841 1.72e-13

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 74.28  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   562 NRIATVEEDCQKMRelkaRAeaadiaksqFLATVSHEIRTPMNGVLGMLKMLMD--TDLDAKQMDYAQTAHGSgkdLTSL 639
Cdd:PRK10549  227 NQLASTLEKNEQMR----RD---------FMADISHELRTPLAVLRGELEAIQDgvRKFTPESVASLQAEVGT---LTKL 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   640 INEVLDQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdvVVGDPSRFRQIITNLVGNSIKFT 719
Cdd:PRK10549  291 VDDLHQLSLSDEGALAYRKTPVDLVPLLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYT 368
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   720 QERGHIFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDT 799
Cdd:PRK10549  369 DSGGSLHISAEQRDK--------------------------------------------------------TLRLTFADS 392
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 18421494   800 GVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVE 841
Cdd:PRK10549  393 APGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVE 434
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
593-859 4.38e-13

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 72.90  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   593 ATVSHEIRTPMNGVLGMLKMLMD-TDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLElenvPFDMRFILDNVS 671
Cdd:PRK10364  242 AGVAHEIRNPLSSIKGLAKYFAErAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQ----AVDLNDLINHSL 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   672 SLLSGKANEKGIELAVYVSSQVPDVVVgDPSRFRQIITNLVGNSIKFTQERGHIFISVhladevkepltiedavlkqrla 751
Cdd:PRK10364  318 QLVSQDANSREIQLRFTANDTLPEIQA-DPDRLTQVLLNLYLNAIQAIGQHGVISVTA---------------------- 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   752 lgcSESGetvsgfpavnawgswknfktcystesqnsDQIKLLVTveDTGVGIPVDAQGRIFTPFMQADSStsrtygGTGI 831
Cdd:PRK10364  375 ---SESG-----------------------------AGVKISVT--DSGKGIAADQLEAIFTPYFTTKAE------GTGL 414
                         250       260
                  ....*....|....*....|....*...
gi 18421494   832 GLSISKRLVELMQGEMGFVSEPGIGSTF 859
Cdd:PRK10364  415 GLAVVHNIVEQHGGTIQVASQEGKGATF 442
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
1037-1165 1.07e-12

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: 65.73  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAML-KPPHNFDACFMDLQMPEMDGFEATRRVRElereinkkiasg 1115
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLrENKDEFDLVITDVHMPDMDGFEFLELIRL------------ 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 18421494 1116 evsaEMfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVL 1165
Cdd:cd17584   69 ----EM-------DLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
574-862 2.40e-12

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 70.26  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  574 MRELKARAEAADIAKSQflatvSHEIRTPMNGVLGMLKMlmdtdldaKQMDYAQTahgsgkdltsLINEVLD--QAKIES 651
Cdd:COG3290  180 EEELEGVKELAEALRAQ-----RHDFRNHLHTISGLLQL--------GEYDEALE----------YIDEISEelQELIDS 236
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  652 GRLELENVpfdmrfildNVSSLLSGK---ANEKGIELAVYVSSQVPDVVVGDPSrFRQIITNLVGNSI----KFTQERGH 724
Cdd:COG3290  237 LLSRIGNP---------VLAALLLGKaarARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeaveKLPEEERR 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  725 IFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIP 804
Cdd:COG3290  307 VELSIRDDGD--------------------------------------------------------ELVIEVEDSGPGIP 330
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  805 VDAQGRIFTP-FmqadssTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:COG3290  331 EELLEKIFERgF------STKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVR 383
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
792-862 2.79e-12

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: 63.99  E-value: 2.79e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494  792 LLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16939   31 LTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVALWHGGHVECDDSELGGACFRLT 101
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
1035-1108 3.10e-12

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 64.16  E-value: 3.10e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHnFDACFMDLQMPEMDGFEATRRVRELEREI 1108
Cdd:cd17554    1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESED-PDLVILDIKMPGMDGLETLRKIREKKPDL 73
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
579-853 3.91e-12

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 70.19  E-value: 3.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   579 ARAEAADIAKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMD---YAQTAHGSgkDLTSLINEVLDQAKIESGRLE 655
Cdd:PRK09835  253 ERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEdvlYSNLEELT--RMAKMVSDMLFLAQADNNQLI 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   656 LENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSsqvPDVVVGDPSRFRQIITNLVGNSIKFTQErGHIfISVHladev 735
Cdd:PRK09835  331 PEKKMLDLADEVGKVFDFFEAWAEERGVELRFVGD---PCQVAGDPLMLRRAISNLLSNALRYTPA-GEA-ITVR----- 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   736 kepltiedavlkqrlalgCSESGETVsgfpavnawgswknfktcystesqnsdqiklLVTVEDTGVGIPVDAQGRIFTPF 815
Cdd:PRK09835  401 ------------------CQEVDHQV-------------------------------QLVVENPGTPIAPEHLPRLFDRF 431
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 18421494   816 MQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEP 853
Cdd:PRK09835  432 YRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA 469
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
784-847 4.30e-12

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: 63.50  E-value: 4.30e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494  784 SQNSDQIKLlvTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEM 847
Cdd:cd16949   25 SQDGDQWTI--TITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGGKI 86
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
1037-1159 4.66e-12

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


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 63.92  E-value: 4.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAML----------KPPHNFDACFMDLQMPEMDGFEATRRVREler 1106
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLgledeedssnFNEPKVNMIITDYCMPGMTGYDLLKKVKE--- 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1107 einkkiaSGEVSaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:cd17581   78 -------SSALK----------EIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
700-853 1.32e-11

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: 62.48  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  700 DPSRFRQIITNLVGNSIKFTQERGHIFISVhladevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktc 779
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRA-------------------------------------------------- 30
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494  780 ysteSQNSDQIKLlvTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEP 853
Cdd:cd16946   31 ----AQTPQEVRL--DVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAICHNIALAHGGTISAEHSP 98
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
1037-1090 1.71e-11

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.27  E-value: 1.71e-11
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....
gi 18421494    1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMP 1090
Cdd:smart00448    3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLK-EEKPDLILLDIMMP 55
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
1037-1169 2.09e-11

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: 62.14  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRvaegALKKY------GAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRELerei 1108
Cdd:cd17535    1 VLIVDDHPLVRE----GLRRLlesepdIEVVGEAADGEEALALLRelRP---DVVLMDLSMPGMDGIEALRRLRRR---- 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1109 nkkiasgevsaemfckfsSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17535   70 ------------------YPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
1035-1169 2.31e-11

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: 62.04  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAMLK--PPhnfDACFMDLQMP-EMDGFEATRRvrelereINK 1110
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGyEVVGIADSGEEAIELAEenKP---DLILMDINLKgDMDGIEAARE-------IRE 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1111 KiasgevsaemfckfssWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17534   71 K----------------FDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
1037-1174 2.52e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 67.57  E-value: 2.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAM--LKPPhnfDACFMDLQMPEMDGFEATRRVRELEREinkkias 1114
Cdd:PRK11361    7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLfaDIHP---DVVLMDIRMPEMDGIKALKEMRSHETR------- 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1115 gevsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:PRK11361   77 ---------------TPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDELNLIVQRALQ 121
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
1035-1173 2.86e-11

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


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 61.53  E-value: 2.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAM---LKPphnfDACFMDLQMPEMDGFEATrrvreleREINK 1110
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGyEVVGEAANGEEAVEKykeLKP----DLVTMDITMPEMDGIEAL-------KEIKK 69
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1111 KIASGEVsaemfckfsswhVPILAMTAdviQATHEECMKCGMDGYVSKPFEEEVLYTAVARFF 1173
Cdd:cd17542   70 IDPNAKV------------IMCSAMGQ---EEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
1037-1174 3.11e-11

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 64.84  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGA--IVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkias 1114
Cdd:COG3279    4 ILIVDDEPLARERLERLLEKYPDleVVGEASNGEEALELLEE-HKPDLVFLDIQMPGLDGFELARQLRELDP-------- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1115 gevsaemfckfsswHVPILAMTAD---VIQATHEECMkcgmdGYVSKPFEEEVLYTAVARFFE 1174
Cdd:COG3279   75 --------------PPPIIFTTAYdeyALEAFEVNAV-----DYLLKPIDEERLAKALEKAKE 118
PRK10490 PRK10490
sensor protein KdpD; Provisional
577-862 3.30e-11

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 67.75  E-value: 3.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   577 LKARAEAADIA------KSQFLATVSHEIRTPMNGVLGMLKMLMdTDLDAKQMDYAQTAHGSGKDL---TSLINEVLDQA 647
Cdd:PRK10490  647 LTASEEQARLAsereqlRNALLAALSHDLRTPLTVLFGQAEILT-LDLASEGSPHARQASEIRQQVlntTRLVNNLLDMA 725
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   648 KIESG----RLE---LENVpfdmrfildnVSSLLSGKANE-KGIELAVYVSSQVPdVVVGDPSRFRQIITNLVGNSIKFT 719
Cdd:PRK10490  726 RIQSGgfnlRKEwltLEEV----------VGSALQMLEPGlSGHPINLSLPEPLT-LIHVDGPLFERVLINLLENAVKYA 794
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   720 QERGHIFISVHLADEvkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDT 799
Cdd:PRK10490  795 GAQAEIGIDAHVEGE--------------------------------------------------------RLQLDVWDN 818
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494   800 GVGIPVDAQGRIFTPFMQADSSTSrtYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:PRK10490  819 GPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVT 879
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
1037-1172 3.91e-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: 61.19  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLkPPHNFDACFMDLQMPEMDGFEATRRVRElereiNKKIAsge 1116
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAML-AEHRPTLVISDIVMPEMDGYELCRKIKS-----DPDLK--- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1117 vsaemfckfsswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:cd17598   72 ------------DIPVILLTTlsdprDVIRG-----LECGADNFITKPYDEKYLLSRIKYI 115
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
1035-1172 6.03e-11

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: 60.63  E-value: 6.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKK-YGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREinkkia 1113
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPAdWDVEITFAENGEEALEILRE-GRIDVLFLDLTMPVMDGYEVLEALPVEQLE------ 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1114 sgevsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:cd17593   74 ----------------TKVIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQLLEEL 116
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
1037-1171 9.02e-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: 60.23  E-value: 9.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHNFDACFMDLQMPEMDGFEATRRVRElereinkkiasge 1116
Cdd:cd17544    3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIRK------------- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494 1117 vsaemfcKFSSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:cd17544   70 -------KYSRDQLAIIGISASGDNALSARFIKAGANDFLTKPFLPEEFYCRVTQ 117
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
1037-1120 1.11e-10

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: 59.44  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHNFDACFMDLQMPEMDGFEATRRVRELEREINKKIASGE 1116
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISGG 81

                 ....
gi 18421494 1117 VSAE 1120
Cdd:cd18160   82 AAAA 85
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
795-861 1.64e-10

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: 59.14  E-value: 1.64e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494  795 TVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSF 861
Cdd:cd16952   36 SVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTC 102
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
594-847 1.85e-10

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 64.87  E-value: 1.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   594 TVSHEIRTPMNGVLGMLKmLMDTDLDAKQMD-YAQTAHGSGKDLTSLINEVLDQAKIESgRLELENV-PFDMRFILDNVS 671
Cdd:PRK11100  262 TLTHELKSPLAAIRGAAE-LLQEDPPPEDRArFTGNILTQSARLQQLIDRLLELARLEQ-RQELEVLePVALAALLEELV 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   672 SLLSGKANEKGIELAVyvssQVPDVVV-GDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEvkepltiedavlkqrl 750
Cdd:PRK11100  340 EAREAQAAAKGITLRL----RPDDARVlGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGE---------------- 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   751 algcsesgetvsgfpavnawgswknfktcystesqnsdQIKLlvTVEDTGVGIPVDAQGRIFTPFMqadsSTSRTYGG-- 828
Cdd:PRK11100  400 --------------------------------------QVAL--SVEDQGPGIPDYALPRIFERFY----SLPRPANGrk 435
                         250       260
                  ....*....|....*....|
gi 18421494   829 -TGIGLSISKRLVELMQGEM 847
Cdd:PRK11100  436 sTGLGLAFVREVARLHGGEV 455
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
1037-1171 2.01e-10

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: 59.32  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAML--KPPhnfDACFMDLQMPEMDGFEATRRVRELEREinkkias 1114
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVIsgNRP---DAVVLDVMMPRLDGLEVCRRLRAAGND------- 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1115 gevsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17627   71 ---------------LPILVLTARDSVSDRVAGLDAGADDYLVKPFALEEL---LAR 109
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
697-856 5.87e-10

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: 57.80  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  697 VVGDPSRFRQIITNLVGNSIKFTQERGHIFISVhladevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknf 776
Cdd:cd16940    7 VQGDALLLFLLLRNLVDNAVRYSPQGSRVEIKL----------------------------------------------- 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  777 ktcystESQNSDQIKllvtVEDTGVGIPVDAQGRIFTPFMQADSstsRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIG 856
Cdd:cd16940   40 ------SADDGAVIR----VEDNGPGIDEEELEALFERFYRSDG---QNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGG 106
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
1037-1103 6.26e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 58.17  E-value: 6.26e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAI--VTCVESGKAALAM---LKPphnfDACFMDLQMPEMDGFEATRRVRE 1103
Cdd:cd17541    3 VLIVDDSAVMRKLLSRILESDPDIevVGTARDGEEALEKikeLKP----DVITLDIEMPVMDGLEALRRIMA 70
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
792-854 7.47e-10

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: 57.41  E-value: 7.47e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494  792 LLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTyGGTGIGLSISKRLVELMQGEMGFVSEPG 854
Cdd:cd16918   44 LRVSVIDNGPGIPPDLQDTIFYPMV-----SGRE-NGTGLGLAIAQNIVSQHGGVIECDSQPG 100
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
1034-1171 7.77e-10

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: 59.16  E-value: 7.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1034 EKQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEreinkkia 1113
Cdd:COG4567    4 DRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQ-APPDYAVLDLRLGDGSGLDLIEALRERD-------- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1114 sgevsAEMfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:COG4567   75 -----PDA---------RIVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALER 118
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
1037-1165 8.85e-10

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 57.29  E-value: 8.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVV-DDNLVNRRVAEgALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasg 1115
Cdd:cd19934    1 LLLVeDDALLAAQLKE-QLSDAGYVVDVAEDGEEALFQGEE-EPYDLVVLDLGLPGMDGLSVLRRWRSEGRAT------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1116 evsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFE-EEVL 1165
Cdd:cd19934   72 ---------------PVLILTARDSWQDKVEGLDAGADDYLTKPFHiEELL 107
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
1037-1165 1.28e-09

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: 56.72  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNlvnRRVAEG---ALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinkkia 1113
Cdd:cd17624    1 ILLVEDD---ALLGDGlktGLRKAGYAVDWVRTGAEAEAALAS-GPYDLVILDLGLPDGDGLDLLRRWRR---------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1114 sgevsaemfckfSSWHVPILAMTA-----DVIqatheECMKCGMDGYVSKPFE-EEVL 1165
Cdd:cd17624   67 ------------QGQSLPVLILTArdgvdDRV-----AGLDAGADDYLVKPFAlEELL 107
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
791-861 1.96e-09

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: 55.93  E-value: 1.96e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494  791 KLLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTYG-GTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSF 861
Cdd:cd16976   34 RLVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
788-862 2.22e-09

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: 56.75  E-value: 2.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18421494  788 DQIKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:cd16947   49 DEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVT 123
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
1035-1161 2.54e-09

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: 56.41  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGA-IVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRElereinkk 1111
Cdd:cd17552    2 KRILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGLEKAAteQP---DAILLDVMMPDMDGLATLKKLQA-------- 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 18421494 1112 iasgevsaemfcKFSSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFE 1161
Cdd:cd17552   71 ------------NPETQSIPVILLTAKAQPSDRQRFASLGVAGVIAKPFD 108
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
1037-1171 4.00e-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: 55.44  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREinkkiasge 1116
Cdd:cd17615    2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAARE-FRPDAVVLDIMLPDMDGLEVLRRLRADGPD--------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1117 vsaemfckfsswhVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFE-EEVlytaVAR 1171
Cdd:cd17615   72 -------------VPVLFLTAkdsveDRIAG-----LTAGGDDYVTKPFSlEEV----VAR 110
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
1037-1122 7.46e-09

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 55.28  E-value: 7.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAI--VTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRV-RELEREINKKIA 1113
Cdd:COG2197    4 VLIVDDHPLVREGLRALLEAEPDIevVGEAADGEEALELLEE-LRPDVVLLDIRMPGMDGLEALRRLlTPREREVLRLLA 82
                         90
                 ....*....|...
gi 18421494 1114 SG----EVSAEMF 1122
Cdd:COG2197   83 EGlsnkEIAERLG 95
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
1036-1174 7.47e-09

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: 55.11  E-value: 7.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1036 QILVVDDNLVNRRVAEGALKKYG--AIVTCVESGKAALAMLKPPHNFDAC------FMDLQMPEMDGFEATRRVRELERe 1107
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADAprpdliLLDLNMPRMDGFEVLREIKADPD- 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1108 inkkiasgevsaemFCkfsswHVPILAMTA-----DViqathEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:cd17557   80 --------------LR-----RIPVVVLTTsdaeeDI-----ERAYELGANSYIVKPVDFEEFVEAIRSLGE 127
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
596-860 7.49e-09

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 59.93  E-value: 7.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   596 SHEIRTPMNGVLGMLKMLMDTDLDakqmDY-AQTAHGSGKDLTSLINevldqaKIESgrlelenvPFDMRFILDNVSsll 674
Cdd:PRK11086  347 SHEFMNKLHVILGLLHLKSYDQLE----DYiLKTANNYQEEIGSLLG------KIKS--------PVIAGFLLGKIS--- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   675 sgKANEKGIELAVYVSSQVPDVvvGDPSRFRQIIT---NLVGNSIkftqerghifisvhladevkepltieDAVLKQrla 751
Cdd:PRK11086  406 --RARELGITLIISEDSQLPDS--GDEDQVHELITilgNLIENAL--------------------------EAVGGE--- 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   752 lgcsESGETVSGFPAVNAWgswknfktcystesqnsdqikLLVTVEDTGVGIPVDAQGRIFTpfmQADSSTSRtygGTGI 831
Cdd:PRK11086  453 ----EGGEISVSLHYRNGW---------------------LHCEVSDDGPGIAPDEIDAIFD---KGYSTKGS---NRGV 501
                         250       260
                  ....*....|....*....|....*....
gi 18421494   832 GLSISKRLVELMQGEMGFVSEPGIGSTFS 860
Cdd:PRK11086  502 GLYLVKQSVENLGGSIAVESEPGVGTQFF 530
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
1037-1121 9.61e-09

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: 54.31  E-value: 9.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--------PPHNFDACFMDLQMPEMDGFEATRRVRELEREI 1108
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                         90
                 ....*....|....*...
gi 18421494 1109 NKKIA-----SGEVSAEM 1121
Cdd:cd19924   81 NIPVIlnsslSGEFSRAR 98
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
1037-1171 1.58e-08

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: 54.03  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPphNFDACFM-DLQMPEMDGFEATRRVRELEREInkkiasg 1115
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSP--DFPGVVIsDIRMPGMDGLELLAQIRELDPDL------- 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1116 evsaemfckfsswhvPILAMTA--DV---IQAtheecMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:cd17549   72 ---------------PVILITGhgDVpmaVEA-----MRAGAYDFLEKPFDPERLLDVVRR 112
PRK10610 PRK10610
chemotaxis protein CheY;
1033-1174 1.83e-08

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 54.21  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1033 REKQILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRelereinkk 1111
Cdd:PRK10610    4 KELKFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQA-GGFGFVISDWNMPNMDGLELLKTIR--------- 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18421494  1112 iASGEVSAemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:PRK10610   74 -ADGAMSA----------LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
envZ PRK09467
osmolarity sensor protein; Provisional
592-846 2.06e-08

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 58.00  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   592 LATVSHEIRTP----------MNGVLGMLK--MLMDT-DLDA--KQ-MDYAQTAHG---SGKDLTSLINEVLdQAkiESG 652
Cdd:PRK09467  233 MAGVSHDLRTPltrirlatemMSEEDGYLAesINKDIeECNAiiEQfIDYLRTGQEmpmEMADLNALLGEVI-AA--ESG 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   653 RlelenvpfdmrfildnvssllsgkanEKGIELAVYVSsqvPDVVVGDPSRFRQIITNLVGNSIKFTqeRGHIFISvhla 732
Cdd:PRK09467  310 Y--------------------------EREIETALQPG---PIEVPMNPIAIKRALANLVVNAARYG--NGWIKVS---- 354
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   733 devkepltiedavlkqrlalgcsesgetvSGFPAVNAWgswknfktcystesqnsdqikllVTVEDTGVGIPVDAQGRIF 812
Cdd:PRK09467  355 -----------------------------SGTEGKRAW-----------------------FQVEDDGPGIPPEQLKHLF 382
                         250       260       270
                  ....*....|....*....|....*....|....
gi 18421494   813 TPFMQADssTSRTYGGTGIGLSISKRLVELMQGE 846
Cdd:PRK09467  383 QPFTRGD--SARGSSGTGLGLAIVKRIVDQHNGK 414
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
792-860 2.08e-08

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: 53.54  E-value: 2.08e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  792 LLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTYG-GTGIGLSISKRLVELMQGEMGFVSEPGIGSTFS 860
Cdd:cd16919   48 VCLEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVR 112
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
591-846 3.62e-08

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: 57.83  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    591 FLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELENVPFDMRFILdnv 670
Cdd:TIGR03785  488 MSSRLSHELRTPVAVVRSSLENLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSEVL--- 564
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    671 SSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISVHLADEvkepltiedavlkqrl 750
Cdd:TIGR03785  565 SGCMQGYQMTYPPQRFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKS---------------- 628
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494    751 algcsesgetvsgfpavnawgswknfktcystesqnsdqiKLLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTG 830
Cdd:TIGR03785  629 ----------------------------------------HALLTVSNEGPPLPEDMGEQLFDSMVSVRDQGAQDQPHLG 668
                          250
                   ....*....|....*.
gi 18421494    831 IGLSISKRLVELMQGE 846
Cdd:TIGR03785  669 LGLYIVRLIADFHQGR 684
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
1037-1171 3.76e-08

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: 52.59  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREINKKIASGe 1116
Cdd:cd17555    3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRS-EQPDLVLCDLRMPEMDGLEVLKQITKESPDTPVIVVSG- 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494 1117 vsaemfckfsswhvpiLAMTADVIQAtheecMKCGMDGYVSKPFEE-EVLYTAVAR 1171
Cdd:cd17555   81 ----------------AGVMSDAVEA-----LRLGAWDYLTKPIEDlAVLEHAVRR 115
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
1037-1171 5.82e-08

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: 52.34  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNlvnRRVAEGaLKK------YGA-IVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELerein 1109
Cdd:cd17536    1 VLIVDDE---PLIREG-LKKlidweeLGFeVVGEAENGEEALELIEE-HKPDIVITDIRMPGMDGLELIEKIREL----- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1110 kkiasgevsaemfckfsSWHVPILAMTAdviqatHEE------CMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:cd17536   71 -----------------YPDIKIIILSG------YDDfeyaqkAIRLGVVDYLLKPVDEEELEEALEK 115
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
1036-1170 6.98e-08

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 56.19  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1036 QILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasg 1115
Cdd:PRK10365    7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVRE-QVFDLVLCDVRMAEMDGIATLKEIKALNPAI------- 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  1116 evsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFE----EEVLYTAVA 1170
Cdd:PRK10365   79 ---------------PVLIMTAYSSVETAVEALKTGALDYLIKPLDfdnlQATLEKALA 122
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
796-847 1.32e-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: 50.91  E-value: 1.32e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18421494  796 VEDTGVGIPVDAQGRIFTPFMQADSStsRTYGGTGIGLSISKRLVELMQGEM 847
Cdd:cd16950   35 VLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIVQRISDAHGGSL 84
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
1037-1103 1.33e-07

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: 51.43  E-value: 1.33e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHnFDACFMDLQMPEMDGFEATRRVRE 1103
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQP-PDVVLLDLKLPDMSGMEILKWIQE 66
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
1035-1171 2.21e-07

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: 50.49  E-value: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYG-AIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinKKIA 1113
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGyEVVGEASDGEEAVELAKK-HKPDLVIMDVKMPRLDGIEAAKIITS------ENIA 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1114 sgevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLY----TAVAR 1171
Cdd:cd19932   74 -----------------PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDLIpaieMAIAR 118
pleD PRK09581
response regulator PleD; Reviewed
1037-1169 2.43e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 54.52  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLVNRRVAEGAL-KKYGAIVTCvESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereiNKKIAsg 1115
Cdd:PRK09581    5 ILVVDDIPANVKLLEAKLlAEYYTVLTA-SSGAEAIAICER-EQPDIILLDVMMPGMDGFEVCRRLKS-----DPATT-- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  1116 evsaemfckfsswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVLYTAV 1169
Cdd:PRK09581   76 -------------HIPVVMVTAlddpeDRVRG-----LEAGADDFLTKPINDVALFARV 116
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
1038-1161 2.91e-07

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: 50.30  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1038 LVVDDNLVNRRVAEgALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinKKIAsgev 1117
Cdd:cd17625    2 VVEDEKDLSEAITK-HLKKEGYTVDVCFDGEEGLEYALS-GIYDLIILDIMLPGMDGLEVLKSLRE------EGIE---- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18421494 1118 saemfckfsswhVPILAMTA-----DVIQATHEecmkcGMDGYVSKPFE 1161
Cdd:cd17625   70 ------------TPVLLLTAldaveDRVKGLDL-----GADDYLPKPFS 101
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
1037-1160 3.32e-07

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 50.11  E-value: 3.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinkkiasge 1116
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEE-EQPDLILLDLMLPEKDGLEVCREVRK------------- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18421494 1117 vsaemfckfsSWHVPILAMTADVIQATHEECMKCGMDGYVSKPF 1160
Cdd:cd17614   67 ----------TSNVPIIMLTAKDSEVDKVLGLELGADDYVTKPF 100
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
1038-1171 3.77e-07

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: 49.96  E-value: 3.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1038 LVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereiNKKIASgev 1117
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKD-EKPDLIILDLMLPGIDGLEVCRILRS-----DPKTSS--- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1118 saemfckfsswhVPILAMTADViqathEECMKC-----GMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd19937   72 ------------IPIIMLTAKG-----EEFDKVlglelGADDYITKPFSPREL---LAR 110
PRK13557 PRK13557
histidine kinase; Provisional
794-925 4.15e-07

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 54.29  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   794 VTVEDTGVGIPVDAQGRIFTPFMqadssTSRTYG-GTGIGLSISKRLVELMQGEMGFVSEPGIGST--FSFTGVfGKAET 870
Cdd:PRK13557  327 IAVTDTGSGMPPEILARVMDPFF-----TTKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTvrLYFPAS-DQAEN 400
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494   871 NTSITKLERFDLAIQEftglRALVIDNRNIRAEVTRYELRRLGISADIVSSLRMA 925
Cdd:PRK13557  401 PEQEPKARAIDRGGTE----TILIVDDRPDVAELARMILEDFGYRTLVASNGREA 451
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
1037-1171 5.08e-07

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: 51.25  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHNfdAC-FMDLQMPEMDGFEATRRVRELEReinkkiasg 1115
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRP--GClLLDVRMPGMSGLELQEELAARGS--------- 70
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1116 evsaemfckfsswHVPILAMT--ADV---IQAtheecMKCG-MDgYVSKPFEEEVLYTAVAR 1171
Cdd:COG4566   71 -------------PLPVIFLTghGDVpmaVRA-----MKAGaVD-FLEKPFDDQALLDAVRR 113
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
1037-1103 5.57e-07

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: 49.42  E-value: 5.57e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRE 1103
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKE-RRPDLVLLDIWLPDMDGLELLKEIKE 66
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
1037-1169 5.76e-07

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: 49.51  E-value: 5.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHNfdACF-MDLQMPEMDGFEATRRVRELEReinkkiasg 1115
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQP--GCLvLDVRMPGMSGLELQDELLARGS--------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494 1116 evsaemfckfsswHVPILAMT--ADVIQATheECMKCGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17537   72 -------------NIPIIFITghGDVPMAV--EAMKAGAVDFLEKPFRDQVLLDAI 112
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
1037-1159 6.08e-07

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: 48.70  E-value: 6.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAAL--AMLKPPhnfDACFMDLQMPEMDGFEATRRVRElereinkkias 1114
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLleAATRKP---DLIILDLGLPDMDGLEVIRRLRE----------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18421494 1115 gevsaemfckfssW-HVPILAMTA-----DVIQAtheecMKCGMDGYVSKP 1159
Cdd:cd17620   67 -------------WsAVPVIVLSArdeesDKIAA-----LDAGADDYLTKP 99
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
1037-1115 9.49e-07

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: 48.50  E-value: 9.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHNFDACFMDLQMP-EMDGFEATRRVRELEREINKKIASG 1115
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
1035-1171 1.19e-06

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: 48.40  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPhNFDACFMDLQMPEMDGFEATRRVR--ELEREInkki 1112
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEP-RPDLILLDWMLPGGSGIQFIRRLKrdEMTRDI---- 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1113 asgevsaemfckfsswhvPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17618   76 ------------------PIIMLTARGEEEDKVRGLEAGADDYITKPFSPREL---VAR 113
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
1035-1169 1.71e-06

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: 48.17  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREINKKIAS 1114
Cdd:cd17569    1 PTILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQ-EPVDVVISDQRMPGMDGAELLKRVRERYPDTVRILLT 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494 1115 GevsaemfckFSSwhvpilamTADVIQATHEecmkCGMDGYVSKPFEEEVLYTAV 1169
Cdd:cd17569   80 G---------YAD--------LDAAIEAINE----GEIYRFLTKPWDDEELKETI 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
1035-1161 2.25e-06

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: 47.65  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRElereinkki 1112
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALAssQP---DVLISDIRMPGMDGLALLAQIKQ--------- 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18421494 1113 asgevsaemfcKFSswHVPILAMTA----DVIQATHEEcmkcGMDGYVSKPFE 1161
Cdd:cd19919   69 -----------RHP--DLPVIIMTAhsdlDSAVSAYQG----GAFEYLPKPFD 104
fixJ PRK09390
response regulator FixJ; Provisional
1039-1174 2.38e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 49.62  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1039 VVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLkPPHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasgevs 1118
Cdd:PRK09390    8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDAL-PGLRFGCVVTDVRMPGIDGIELLRRLKARGSPL---------- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494  1119 aemfckfsswhvPILAMT--ADVIQATheECMKCGMDGYVSKPFEEEVLYTAVARFFE 1174
Cdd:PRK09390   77 ------------PVIVMTghGDVPLAV--EAMKLGAVDFIEKPFEDERLIGAIERALA 120
glnL PRK11073
nitrogen regulation protein NR(II);
796-854 2.60e-06

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 50.85  E-value: 2.60e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494   796 VEDTGVGIPVDAQGRIFTPFMQADSstsrtyGGTGIGLSISKRLVELMQGEMGFVSEPG 854
Cdd:PRK11073  285 IEDNGPGIPPHLQDTLFYPMVSGRE------GGTGLGLSIARNLIDQHSGKIEFTSWPG 337
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
792-860 4.70e-06

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: 46.51  E-value: 4.70e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494  792 LLVTVEDTGVGIPVDAQGRIFtpfmqADSSTSRTYGGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFS 860
Cdd:cd16915   37 LVIEVRDTGPGIAPELRDKVF-----ERGVSTKGQGERGIGLALVRQSVERLGGSITVESEPGGGTTFS 100
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
776-862 8.41e-06

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: 46.47  E-value: 8.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  776 FKTCYS----TESQNSDQIKLlvTVEDTGVGIPVDAQGRIFTPFMQADSSTSrtygGTGIGLSISKRLVELMQGEMGFVS 851
Cdd:cd16954   50 CKWCLEfvevTARQTDGGLHL--IVDDDGPGVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSD 123
                         90
                 ....*....|.
gi 18421494  852 EPGIGSTFSFT 862
Cdd:cd16954  124 SPLGGARFEVV 134
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
1037-1171 1.06e-05

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


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 45.76  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNlvnRRVAEgALKKY----GAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinkki 1112
Cdd:cd17623    1 ILLIDDD---RELTE-LLTEYlemeGFNVRAAHDGEQGLAALLE-GSPDLVVLDVMLPKMNGLDVLKELRK--------- 66
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494 1113 asgevsaemfckfsSWHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17623   67 --------------TSQVPVLMLTArgddiDRILG-----LELGADDYLPKPFNPREL---VAR 108
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
1037-1171 1.25e-05

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: 45.44  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAML--KPPhnfDACFMDLQMPEMDGFEATRRVRElereinkkias 1114
Cdd:cd19939    2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIidEQP---SLVVLDIMLPGMDGLTVCREVRE----------- 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1115 gevsaemfckfsSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd19939   68 ------------HSHVPILMLTARTEEMDRVLGLEMGADDYLCKPFSPREL---LAR 109
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
1037-1165 1.51e-05

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 45.51  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAI-VTCVESGKAALAMLKPPHNfDACFMDLQMPEMDGFEATRRVRELEREINKKIASG 1115
Cdd:cd17530    3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAP-DIIICDLKMPDMDGIEFLRHLAESHSNAAVILMSG 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18421494 1116 evsaemfckfsswhvpilaMTADVIQATHEECMKCGMD--GYVSKPFEEEVL 1165
Cdd:cd17530   82 -------------------LDGGILESAETLAGANGLNllGTLSKPFSPEEL 114
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
1037-1161 1.61e-05

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 45.07  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPPHnFDACFMDLQMPEMDGFEATRRVRELEreinkkiasge 1116
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQD-IDLVLLDINLPGKDGLSLTRELREQS----------- 70
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 18421494 1117 vsaemfckfsswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFE 1161
Cdd:cd17619   71 ------------EVGIILVTGrddevDRIVG-----LEIGADDYVTKPFN 103
PRK13557 PRK13557
histidine kinase; Provisional
1037-1121 1.85e-05

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 48.90  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLvnrRVAEGA---LKKYGAIVTCVESGKAALAMLKPPHNFDACFMDLQMP-EMDGFEATRRVRELEREINKKI 1112
Cdd:PRK13557  418 ILIVDDRP---DVAELArmiLEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIKVLL 494

                  ....*....
gi 18421494  1113 ASGEVSAEM 1121
Cdd:PRK13557  495 TTGYAEASI 503
orf27 CHL00148
Ycf27; Reviewed
1033-1160 3.01e-05

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 47.02  E-value: 3.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1033 REKQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVRelereinkki 1112
Cdd:CHL00148    5 SKEKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFR-KEQPDLVILDVMMPKLDGYGVCQEIR---------- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18421494  1113 asgevsaemfckfSSWHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPF 1160
Cdd:CHL00148   74 -------------KESDVPIIMLTAlgdvsDRITG-----LELGADDYVVKPF 108
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
1037-1165 4.60e-05

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


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 43.81  E-value: 4.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAAL---AMLKPphnfDACFMDLQMPEMDGFEATRRVRelereinkkia 1113
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLeefLQFKP----DLVLLDINLPYFDGFYWCREIR----------- 65
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494 1114 sgevsaemfcKFSswHVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVL 1165
Cdd:cd18159   66 ----------QIS--NVPIIFISSrddnmDQVMA-----INMGGDDYITKPFDLDVL 105
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
587-862 4.60e-05

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 47.62  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   587 AKSQFLATVSHEIRTPMNGVLGMLKMLMDTDLDAKQMDYAQTAHGSGKDLTSLINEVLDQAKIESGRLELENVPFDMRFI 666
Cdd:PRK10618  449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDL 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   667 LDNVSSLLSGKANEKGIELAVYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQeRGHIFISVHLADEVKEPLTIEdavl 746
Cdd:PRK10618  529 IDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTA-YGKITLEVDQDESSPDRLTIR---- 603
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   747 kqrlalgcsesgetvsgfpavnawgswknfktcystesqnsdqikllvtVEDTGVGIPVDAQGRIFTPFMqADSSTSRTY 826
Cdd:PRK10618  604 -------------------------------------------------ILDTGAGVSIKELDNLHFPFL-NQTQGDRYG 633
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 18421494   827 GGTGIGLSISKRLVELMQGEMGFVSEPGIGSTFSFT 862
Cdd:PRK10618  634 KASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYSIH 669
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
1037-1160 4.65e-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: 43.97  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKA-ALAMLKPPHnfDACFMDLQMPEMDGFEATRRVRelereinkkiasg 1115
Cdd:cd17594    2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEeARLMLHRRV--DLVLLDLRLGQESGLDLLRTIR------------- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 18421494 1116 evsaemfckfSSWHVPILAMTADVIQ-ATHEECMKCGMDGYVSKPF 1160
Cdd:cd17594   67 ----------ARSDVPIIIISGDRRDeIDRVVGLELGADDYLAKPF 102
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
792-835 4.97e-05

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 47.23  E-value: 4.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 18421494   792 LLVTVEDTGVGIPVDAQGRIFTPFMQADSSTSRTYGGTGIGLSI 835
Cdd:PRK09470  384 LTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAI 427
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
1036-1171 6.22e-05

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


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 43.61  E-value: 6.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1036 QILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAM---LKPphnfDACFMDLQMPEMDGFEATRRVRElereinkki 1112
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAfreVRP----DLVLLDLMLPGIDGIEVCRQIRA--------- 68
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494 1113 ASGevsaemfckfsswhVPILAMTA-----DVIQAtheecMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17626   69 ESG--------------VPIVMLTAksdtvDVVLG-----LESGADDYVAKPFKPKEL---VAR 110
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
1037-1159 6.54e-05

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: 43.14  E-value: 6.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEReinkkiasge 1116
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQ-YIPDLIISDIIMPGVDGYSLLGKLRKNAD---------- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18421494 1117 vsaemFCkfsswHVPIL-----AMTADVIQAtheecMKCGMDGYVSKP 1159
Cdd:cd19927   70 -----FD-----TIPVIfltakGMTSDRIKG-----YNAGCDGYLSKP 102
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
1035-1104 1.15e-04

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 42.81  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKpPHNFDACFMDLQMPEMDGFEATRRVREL 1104
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAR-EEKPDYAVLDLRLGGDSGLDLIPPLRAL 69
PRK10336 PRK10336
two-component system response regulator QseB;
1037-1160 1.18e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.89  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLVNRRVAEGaLKKYGAIV---TCVESGKAALamLKPPhnFDACFMDLQMPEMDGFEATRRVRELEReinkkia 1113
Cdd:PRK10336    4 LLIEDDMLIGDGIKTG-LSKMGFSVdwfTQGRQGKEAL--YSAP--YDAVILDLTLPGMDGRDILREWREKGQ------- 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18421494  1114 sgevsaemfckfsswHVPILAMTADVIQATHEECMKCGMDGYVSKPF 1160
Cdd:PRK10336   72 ---------------REPVLILTARDALAERVEGLRLGADDYLCKPF 103
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
559-846 1.27e-04

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 46.22  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  559 EAINRIATVEEDCQKMRELKARAEAADIAksQFLATVSHEIRTPMNGVLGMLKMLmDTDLDAKQMDYAQTAHGSGKDLTS 638
Cdd:COG4192  406 EIEERKRIEKNLRQTQDELIQAAKMAVVG--QTMTSLAHELNQPLNAMSMYLFSA-KKALEQENYAQLPTSLDKIEGLIE 482
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  639 LINEVLDQAKIESGRLELENVPFDMRFILDNVSSLLSGKANEKGIELAVYVSSQVPdvvvGDPSRFRQIITNLVGNSIkf 718
Cdd:COG4192  483 RMDKIIKSLRQFSRKSDTPLQPVDLRQVIEQAWELVESRAKPQQITLHIPDDLMVQ----GDQVLLEQVLVNLLVNAL-- 556
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  719 tqerghifisvhlaDEVKEPLTIEDAVLKQrlalgcsesgetvsgfpavnawgswknfktcystesqnsdQIKLLVTVED 798
Cdd:COG4192  557 --------------DAVATQPQISVDLLSN----------------------------------------AENLRVAISD 582
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 18421494  799 TGVGIPVdaQGRIFTPFmqadssTSRTYGGTGIGLSISKRLVELMQGE 846
Cdd:COG4192  583 NGNGWPL--VDKLFTPF------TTTKEVGLGLGLSICRSIMQQFGGD 622
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
1036-1171 1.60e-04

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 42.37  E-value: 1.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1036 QILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRelereinkkia 1113
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRhtPP---DLILLDLMLPGTDGLTLCREIR----------- 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1114 sgevsaemfcKFSSwhVPILAMTADVIQATHEECMKCGMDGYVSKPFE-EEVlytaVAR 1171
Cdd:cd19938   67 ----------RFSD--VPIIMVTARVEEIDRLLGLELGADDYICKPYSpREV----VAR 109
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
780-862 1.76e-04

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: 41.89  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  780 YSTESQN------SDQIKLLVTVEDTGVGIPVDAQGRIFTPFMQadSSTSRTYG-GTGIGLSISKRLVELMQGEMGFVSE 852
Cdd:cd16948   20 YSKQGGKieiyseTNEQGVVLSIKDFGIGIPEEDLPRVFDKGFT--GENGRNFQeSTGMGLYLVKKLCDKLGHKIDVESE 97
                         90
                 ....*....|
gi 18421494  853 PGIGSTFSFT 862
Cdd:cd16948   98 VGEGTTFTIT 107
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
1035-1172 2.05e-04

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: 42.16  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRELEREINkki 1112
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTkeRP---DLVLLDMKIPGMDGIEILKRMKVIDENIR--- 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18421494 1113 asgevsaemfckfsswhvpILAMTA----DVIQatheECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:cd17553   75 -------------------VIIMTAygelDMIQ----ESKELGALTHFAKPFDIDEIRDAVKKY 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
1037-1174 2.13e-04

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: 42.14  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTC--VESGKAALAMLKPpHNFDACFMDLQMPEMDGFEAtrrvrelereinkkias 1114
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEE-LKPDVVFLDIQMPGLDGLEL----------------- 62
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1115 gevsAEMFCKFSswHVPIL---------AMTADVIQATheecmkcgmdGYVSKPFEEEVLYTAVARFFE 1174
Cdd:cd17532   63 ----AKKLSKLA--KPPLIvfvtaydeyAVEAFELNAV----------DYLLKPFSEERLAEALAKLRK 115
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
590-846 2.27e-04

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 44.96  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   590 QFLATVSHEIRTPMNGV------------------LGMLKMLMDTDLDAKQMDYAQTAHGSGKDLT-SLINEVLDQAKIE 650
Cdd:PRK10755  139 LFTADVAHELRTPLAGIrlhlellekqhhidvaplIARLDQMMHTVEQLLQLARAGQSFSSGHYQTvKLLEDVILPSQDE 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   651 -SGRLELENVPFDmrfildnvssllsgkanekgielavYVSSQVPDVVVGDPSRFRQIITNLVGNSIKFTQERGHIFISV 729
Cdd:PRK10755  219 lSEMLEQRQQTLL-------------------------LPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTITIKL 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494   730 HLADEvkepltiedavlkqrlalGCSesgetvsgfpavnawgswknfktcystesqnsdqikllVTVEDTGVGIPVDAQG 809
Cdd:PRK10755  274 SQEDG------------------GAV--------------------------------------LAVEDEGPGIDESKCG 297
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 18421494   810 RIFTPFMQADSStsrtYGGTGIGLSISKRLVELMQGE 846
Cdd:PRK10755  298 ELSKAFVRMDSR----YGGIGLGLSIVSRITQLHHGQ 330
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
1037-1137 2.77e-04

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: 41.27  E-value: 2.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNlvnRRVAEgALKK----YGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRElereinkki 1112
Cdd:cd19935    1 ILVVEDE---KKLAE-YLKKglteEGYAVDVAYDGEDGLHLALT-NEYDLIILDVMLPGLDGLEVLRRLRA--------- 66
                         90       100
                 ....*....|....*....|....*
gi 18421494 1113 asgevsaemfckfSSWHVPILAMTA 1137
Cdd:cd19935   67 -------------AGKQTPVLMLTA 78
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
1036-1160 2.86e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 43.80  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1036 QILVVDDNlvnRRVAEG---ALKKYGAIVTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRELEREink 1110
Cdd:PRK11083    5 TILLVEDE---QAIADTlvyALQSEGFTVEWFERGLPALDKLRqqPP---DLVILDVGLPDISGFELCRQLLAFHPA--- 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494  1111 kiasgevsaemfckfsswhVPILAMTAdviqaTHEEC-----MKCGMDGYVSKPF 1160
Cdd:PRK11083   76 -------------------LPVIFLTA-----RSDEVdrlvgLEIGADDYVAKPF 106
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
700-854 2.88e-04

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: 41.29  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  700 DPSRFRQIITNLVGNSIKFTQERGHIFISVHLadevkepltiedavlkqrlalgcsesgetvsgfpavnawgswknfktc 779
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEA------------------------------------------------ 32
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494  780 ystesqNSDQIKLLVtvEDTGVGIPVDAQGRIFTPFMqadsSTSRTYGG---TGIGLSISKRLVELMQGEMGFVSEPG 854
Cdd:cd16945   33 ------DTEGIELLV--FDEGSGIPDYALNRVFERFY----SLPRPHSGqksTGLGLAFVQEVAQLHGGRITLRNRPD 98
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
1037-1159 2.89e-04

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: 41.20  E-value: 2.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELerEINKkiasge 1116
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLN-SKPDLILIDIDMPDLDGYELCSLLRKS--SALK------ 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18421494 1117 vsaemfckfsswHVPILAMTA-----DVIQATheecmKCGMDGYVSKP 1159
Cdd:cd17602   72 ------------DTPIIMLTGkdglvDRIRAK-----MAGASGYLTKP 102
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
1037-1171 3.26e-04

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


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 41.63  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRELEREINKKIASGe 1116
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKL-YDYDIILLDLNLPDMSGYEVLRTLRLAKVKTPILILSG- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18421494 1117 vsaemfckfsswhvpiLAMTADVIQAtheecMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17616   79 ----------------LADIEDKVKG-----LGFGADDYMTKPFHKDEL---VAR 109
ompR PRK09468
osmolarity response regulator; Provisional
1037-1160 3.81e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 43.42  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAaLAMLKPPHNFDACFMDLQMPEMDGFEATRRVRELEREInkkiasge 1116
Cdd:PRK09468    8 ILVVDDDMRLRALLERYLTEQGFQVRSAANAEQ-MDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPT-------- 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18421494  1117 vsaemfckfsswhvPILAMTA-----DVIQAtheecMKCGMDGYVSKPF 1160
Cdd:PRK09468   79 --------------PIIMLTAkgeevDRIVG-----LEIGADDYLPKPF 108
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
1037-1159 3.90e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 44.10  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1037 ILVVDDNLVNRRVAEGALKKYGAI--VTCVESGKAALAMLK--PPhnfDACFMDLQMPEMDGFEATRRVRelereinkki 1112
Cdd:PRK12555    3 IGIVNDSPLAVEALRRALARDPDHevVWVATDGAQAVERCAaqPP---DVILMDLEMPRMDGVEATRRIM---------- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 18421494  1113 asgevsAEMFCkfsswhvPILAMTADVIQATHE--ECMKCGMDGYVSKP 1159
Cdd:PRK12555   70 ------AERPC-------PILIVTSLTERNASRvfEAMGAGALDAVDTP 105
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
780-862 5.32e-04

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 40.45  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  780 YSTESQNSDQIKllVTVEDTGVGIPVDAQGRIFTPFMQADssTSRTYGGTGIGLSISKRLVELMQGEMGFVSEpGIGSTF 859
Cdd:cd16923   23 YITSFLTDDVVN--IMFKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGLSIAKAIIELHGGSASAEYD-DNHDLF 97

                 ...
gi 18421494  860 SFT 862
Cdd:cd16923   98 KVR 100
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
1037-1172 6.14e-04

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: 40.69  E-value: 6.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTC--VESGKAALAMLKPPHnFDACFMDLQMPEMDGFEATRRVRELEREinkkias 1114
Cdd:cd19925    3 VLIVEDDPMVAEIHRAYVEQVPGFTVIgtAGTGEEALKLLKERQ-PDLILLDIYLPDGNGLDLLRELRAAGHD------- 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 18421494 1115 gevsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLYTAVARF 1172
Cdd:cd19925   75 ---------------VDVIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
1060-1103 6.32e-04

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


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 40.72  E-value: 6.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 18421494 1060 IVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVRE 1103
Cdd:cd19930   26 VVAQASNGQEALRLVLK-HSPDVAILDIEMPGRTGLEVAAELRE 68
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
791-857 7.05e-04

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: 40.21  E-value: 7.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494  791 KLLVTVEDTGVGIPVDAQGRIFTPFMqadssTSRTyGGTGIGLSISKRLVELMQGEMGFVSEPGIGS 857
Cdd:cd16944   41 RIVLIVCDNGKGFPREMRHRATEPYV-----TTRP-KGTGLGLAIVKKIMEEHGGRISLSNREAGGA 101
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
1035-1171 8.88e-04

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: 40.44  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1035 KQILVVDDNLVNRRVAEgALKKYGAIVTCVESGKAALAML---KPphnfDACFMDLQMPEMDGFEATRRVRelereinkk 1111
Cdd:cd17622    2 RILLVEDDPKLARLIAD-FLESHGFNVVVEHRGDRALEVIareKP----DAVLLDIMLPGIDGLTLCRDLR--------- 67
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1112 iasgevsaemfckfSSWHVPILAMTADVIQATHEECMKCGMDGYVSKPFEEEVLytaVAR 1171
Cdd:cd17622   68 --------------PKYQGPILLLTALDSDIDHILGLELGADDYVVKPVEPAVL---LAR 110
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
1031-1171 9.84e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 41.94  E-value: 9.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1031 LLRE--KQILVVDDNLvnRRVAEGAlkkygaivtcveSGKAALAM---LKPphnfDACFMDLQMPEMDGFEATRRVRelE 1105
Cdd:PRK10651   17 MLRTgvKQLISMAPDI--TVVGEAS------------NGEQGIELaesLDP----DLILLDLNMPGMNGLETLDKLR--E 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494  1106 REINKKIASGEVSAEmfckfsswhvpilamTADVIQAtheecMKCGMDGYVSKPFEEEVLYTAVAR 1171
Cdd:PRK10651   77 KSLSGRIVVFSVSNH---------------EEDVVTA-----LKRGADGYLLKDMEPEDLLKALQQ 122
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
791-845 1.46e-03

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: 39.48  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18421494  791 KLLVTVEDTGVGIPVDAQGRIFTPFMqADSSTSRTYG-GTGIGLSISKRLVELMQG 845
Cdd:cd16953   33 MVTISVEDEGPGIPQEKLESIFDRFY-TERPANEAFGqHSGLGLSISRQIIEAHGG 87
PRK10816 PRK10816
two-component system response regulator PhoP;
1036-1171 1.78e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 41.26  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494  1036 QILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLKPpHNFDACFMDLQMPEMDGFEATRRVREleREINkkiasg 1115
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNE-HLPDIAIVDLGLPDEDGLSLIRRWRS--NDVS------ 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18421494  1116 evsaemfckfsswhVPILAMTADVIQATHEECMKCGMDGYVSKPFE-EEVlytaVAR 1171
Cdd:PRK10816   73 --------------LPILVLTARESWQDKVEVLSAGADDYVTKPFHiEEV----MAR 111
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
1037-1159 2.19e-03

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 38.92  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAMLK-PPHNFDACFMDLQMPEMDGFEATRRVrelereINKKIasg 1115
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdEQNEIDLILTEVDLPVSSGFKLLSYI------MRHKI--- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18421494 1116 evsaemfCKfsswHVPILAMTADVIQATHEECMKCGMDGYVSKP 1159
Cdd:cd17582   72 -------CK----NIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
1037-1103 2.98e-03

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 38.19  E-value: 2.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18421494 1037 ILVVDDNLVNRRVAEGALKKYGAIVTCVESGKAALAML--KPPhnfDACFMDLQMPEMDGFEATRRVRE 1103
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLnaRPP---DLAILDIKMPRMDGMELLQRLRQ 66
 
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