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Conserved domains on  [gi|18379305|ref|NP_565277|]
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CHASE domain containing histidine kinase protein [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

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List of domain hits

Name Accession Description Interval E-value
PRK11107 super family cl35992
hybrid sensory histidine kinase BarA; Provisional
435-1052 2.30e-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: 359.55  E-value: 2.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   435 EMQ--EL---KVRA-EAADVaKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDR 508
Cdd:PRK11107  273 EIQnvELdlaKKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDF 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   509 AKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFV 588
Cdd:PRK11107  352 SKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDI 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   589 KVHLAEQSKDesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissNVRLMVSIED 668
Cdd:PRK11107  432 LVELRALSNT------------------------------------------------------------KVQLEVQIRD 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   669 TGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKcdKCSAINHmk 748
Cdd:PRK11107  452 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDL--NPNPIID-- 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   749 KPNVEHLpstfKGMKAIVVDAKPVRAAVTRYHMKRLGINVDVVTSLKTAVVAAAAFERNGSPLPTKPQLdmilvekdswi 828
Cdd:PRK11107  528 GLPTDCL----AGKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPL----------- 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   829 stEDNDSEIRLLNSRTNgNVHhkspkLALFATNITNSEfdrAKSAGFADTVIMKPLRASMIgacLQQVLELRKTRQQHPE 908
Cdd:PRK11107  593 --TMLHERLAKAKSMTD-FLI-----LALPCHEQVLAE---QLKQDGADACLSKPLSHTRL---LPALLEPCHHKQPPLL 658
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   909 GSSPATLKSLltgkKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQI 988
Cdd:PRK11107  659 PPTDESRLPL----TVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELI 733
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18379305   989 RmmeketkeKTNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLyKSVAKSFKPNP 1052
Cdd:PRK11107  734 R--------QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAML-KQVLLRYKPGP 788
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
177-359 5.17e-50

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: 174.79  E-value: 5.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    177 SAIDQETFAEYTARTAFERPLLSGVAYAEKVVNFEREMFERQH------NWVIKtmdrgePSPVRDEYAPVIFSQDSVSY 250
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR------PAGDRDEYFPIIYIEPLAGN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    251 --LESLDMMSGEEDRENILRARETGKAVLTSPFRLL--ETHHLGVVLTFPVYKSSLPEnpTVEERIAATAGYLGGAFDVE 326
Cdd:pfam03924   75 nrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRAALLGFVYAPFRID 152
                          170       180       190
                   ....*....|....*....|....*....|...
gi 18379305    327 SLVENLLGQLaGNQAIVVHVYDITNASDPLVMY 359
Cdd:pfam03924  153 DLLEAALLRL-GEDGLDLALYDGTSASAPELLY 184
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
435-1052 2.30e-108

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 359.55  E-value: 2.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   435 EMQ--EL---KVRA-EAADVaKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDR 508
Cdd:PRK11107  273 EIQnvELdlaKKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDF 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   509 AKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFV 588
Cdd:PRK11107  352 SKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDI 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   589 KVHLAEQSKDesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissNVRLMVSIED 668
Cdd:PRK11107  432 LVELRALSNT------------------------------------------------------------KVQLEVQIRD 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   669 TGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKcdKCSAINHmk 748
Cdd:PRK11107  452 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDL--NPNPIID-- 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   749 KPNVEHLpstfKGMKAIVVDAKPVRAAVTRYHMKRLGINVDVVTSLKTAVVAAAAFERNGSPLPTKPQLdmilvekdswi 828
Cdd:PRK11107  528 GLPTDCL----AGKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPL----------- 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   829 stEDNDSEIRLLNSRTNgNVHhkspkLALFATNITNSEfdrAKSAGFADTVIMKPLRASMIgacLQQVLELRKTRQQHPE 908
Cdd:PRK11107  593 --TMLHERLAKAKSMTD-FLI-----LALPCHEQVLAE---QLKQDGADACLSKPLSHTRL---LPALLEPCHHKQPPLL 658
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   909 GSSPATLKSLltgkKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQI 988
Cdd:PRK11107  659 PPTDESRLPL----TVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELI 733
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18379305   989 RmmeketkeKTNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLyKSVAKSFKPNP 1052
Cdd:PRK11107  734 R--------QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAML-KQVLLRYKPGP 788
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
440-1046 2.45e-73

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: 262.79  E-value: 2.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    440 KVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAGKLELE 519
Cdd:TIGR02956  454 RAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSIS 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    520 SVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFVKVHLAEQSKde 599
Cdd:TIGR02956  534 PRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSS-- 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    600 sepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrLMVSIEDTGIGIPLVAQG 679
Cdd:TIGR02956  612 --------------------------------------------------------------LLFEVEDTGCGIAEEEQA 629
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    680 RVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKCDKcsainhmkkpnvehlpstf 759
Cdd:TIGR02956  630 TLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKP------------------- 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    760 kgmkaivvdakpvraavtryhmkrlginvdvvtslktavVAAAAFerngsplptkpqldmilvekdswistedndseirl 839
Cdd:TIGR02956  689 ---------------------------------------AEDSAT----------------------------------- 694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    840 lnsrtngnvhhkspklalfatnitnsefdraksagfaDTVIMKPlrasmigaclqqvlelrktrqqhpegsspatlksll 919
Cdd:TIGR02956  695 -------------------------------------LTVIDLP------------------------------------ 701
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    920 tGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKEkt 999
Cdd:TIGR02956  702 -PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFH-QHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNE-- 777
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 18379305   1000 nlewhLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:TIGR02956  778 -----VKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
433-732 5.82e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 219.78  E-value: 5.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  433 FHEMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDtELSSTQRDYAQTAQVCGKALIALINEVLDRAKIE 512
Cdd:COG0642   93 LLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE-ELDEEQREYLETILRSADRLLRLINDLLDLSRLE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  513 AGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPeIVKGDSGRFRQIIINLVGNSVKFTEKGHIfVKVHL 592
Cdd:COG0642  172 AGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGT-VTVSV 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  593 AEQSKdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIG 672
Cdd:COG0642  250 RREGD---------------------------------------------------------------RVRISVEDTGPG 266
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  673 IPLVAQGRVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG0642  267 IPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
177-359 5.17e-50

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: 174.79  E-value: 5.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    177 SAIDQETFAEYTARTAFERPLLSGVAYAEKVVNFEREMFERQH------NWVIKtmdrgePSPVRDEYAPVIFSQDSVSY 250
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR------PAGDRDEYFPIIYIEPLAGN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    251 --LESLDMMSGEEDRENILRARETGKAVLTSPFRLL--ETHHLGVVLTFPVYKSSLPEnpTVEERIAATAGYLGGAFDVE 326
Cdd:pfam03924   75 nrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRAALLGFVYAPFRID 152
                          170       180       190
                   ....*....|....*....|....*....|...
gi 18379305    327 SLVENLLGQLaGNQAIVVHVYDITNASDPLVMY 359
Cdd:pfam03924  153 DLLEAALLRL-GEDGLDLALYDGTSASAPELLY 184
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
566-735 6.38e-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: 163.05  E-value: 6.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  566 FRQIIINLVGNSVKFTEKGHIFVKVHLAEQSKDEsepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlv 645
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDG---------------------------------------------- 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  646 seeqslsefdissnVRLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHI 725
Cdd:cd16922   35 --------------VQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQ 100
                        170
                 ....*....|
gi 18379305  726 GSTFWFTAVL 735
Cdd:cd16922  101 GSTFTFTLPL 110
CHASE1 COG3614
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
100-380 1.59e-31

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


Pssm-ID: 442832 [Multi-domain]  Cd Length: 588  Bit Score: 131.35  E-value: 1.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  100 HRALLPKALILWIIIVG--FISSGIYQWMDDANKIRREEVLVSMCDQRARMLQDQFSvsvNHVHALAILVSTFHyhkNPS 177
Cdd:COG3614    4 SRSLLRRRLLPLLVLLLglLLTALAWWAVRRAEEQRARARFERLADELASALEERLD---AYEQVLRGLAGLFA---ASD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  178 AIDQETFAEYTARTAFER--PLLSGVAYAEKVVNFEREMFE---RQHNW---VIKtmdrgePSPVRDEYAPVIfsqdsvs 249
Cdd:COG3614   78 DVTRAEFRRYVASLDLLRryPGIQGLGWAPRVPAAERAAFEaaaRAEGFpdfRIR------PAGERDEYFPIT------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  250 YLES----------LDMMSGEEDRENILRARETGKAVLTSPFRLL--ETHHLGVVLTFPVYKSSLPeNPTVEERIAATAG 317
Cdd:COG3614  145 YIEPldarnrralgFDMASEPVRRAAMERARDTGRPAASGPVTLVqeTDGQPGFLLYLPVYRGGAP-PDTVAERRAALRG 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305  318 YLGGAFDVESLVENLLGQLAgNQAIVVHVYDITNASDPLVMY---GNQDEEADRSLSHESKLDFGD 380
Cdd:COG3614  224 FVYAPFRMDDLLAGVLGRLA-DRDLDLRLYDGTDPGPPQLLYdssPAAPAAAAPALSATRTLEVAG 288
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
177-348 8.42e-31

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: 119.36  E-value: 8.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     177 SAIDQETFAEYTARTAFER--PLLSGVAYAEKVVNFEREMFERQ------HNWVIktmdRGEPSPVRDEYAPVIFSQDSV 248
Cdd:smart01079    2 ESVSRAEFRRFALELQLNRrlPGIQGLGWAPRVPPAERAAFEAAlraggpGLFNI----RLAPDGERDEYFVITYIEPLA 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     249 SYLESL--DMMSGEEDRENILRARETGKAVLTSPFRLLETHH--LGVVLTFPVYKSslpeNPTVEERIAATAGYLGGAFD 324
Cdd:smart01079   78 GNEAALglDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGdgRGFLLRLPVYRG----GPPTSTRREALWGFVSAVFR 153
                           170       180
                    ....*....|....*....|....
gi 18379305     325 VESLVENLLGQLAGNQaIVVHVYD 348
Cdd:smart01079  154 LDDLLEGLLGALDLPG-LDLALYD 176
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
924-1045 1.29e-26

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 104.93  E-value: 1.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmeketkektNLEW 1003
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLK-EERPDLILLDINMPGMDGLELLKRIR----------RRDP 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 18379305   1004 HLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVA 1045
Cdd:pfam00072   70 TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
561-732 3.44e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 95.41  E-value: 3.44e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     561 GDSGRFRQIIINLVGNSVKFT-EKGHIFVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswd 639
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGD-------------------------------------------- 36
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     640 sfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSsTSRNYGGTGIGLSISKCLVELMRGQINF 719
Cdd:smart00387   37 ---------------------HVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISV 94
                           170
                    ....*....|...
gi 18379305     720 ISRPHIGSTFWFT 732
Cdd:smart00387   95 ESEPGGGTTFTIT 107
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
427-732 1.46e-12

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 71.21  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   427 VKVEDD-------FHEM----QELKVRAEAADVAKSQFLATVSHEIRTPMNGIlGMLAMLL---DTELSSTQRDYAQTAQ 492
Cdd:NF040691  237 VKGEDDlarlarsFNQMadslQRQIRQLEELSRLQQRFVSDVSHELRTPLTTI-RMAADVIhdsRDDFDPATARSAELLH 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   493 VCGKALIALINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELaVFVSDKVPEIVKGDSGRFRQIIIN 572
Cdd:NF040691  316 TELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVEL-RVDAPGTPVVAEVDPRRVERVLRN 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   573 LVGNSVKFTEKGHIFVKVhlaeqskdesepknalnggvseemivvskqssyntlsgyeAADGRnswdsfkhlvseeqsls 652
Cdd:NF040691  395 LVVNAIEHGEGKPVVVTV----------------------------------------AQDDT----------------- 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   653 efdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:NF040691  418 --------AVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
428-723 1.49e-12

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 71.01  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   428 KVEDDFHEMQELKVRAEAAdvaKSQFLATVSHEIRTPMNGILGMLAMLLD-------TELSSTQRDYAQtaqvcgkaLIA 500
Cdd:NF012163  221 KLAQDFNQLASTLEKNEQM---RRDFMADISHELRTPLAVLRAELEAIQDgirkftpESLDSLQAEVGT--------LTK 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   501 LINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVpeIVKGDSGRFRQIIINLVGNSVKF 580
Cdd:NF012163  290 LVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRY 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   581 TEKGHifvKVHLAEQSKDESepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnv 660
Cdd:NF012163  368 TDSGG---SLHISASQRPKE------------------------------------------------------------ 384
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305   661 rLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRP 723
Cdd:NF012163  385 -VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSP 446
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
435-1052 2.30e-108

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 359.55  E-value: 2.30e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   435 EMQ--EL---KVRA-EAADVaKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDR 508
Cdd:PRK11107  273 EIQnvELdlaKKRAqEAARI-KSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDF 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   509 AKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFV 588
Cdd:PRK11107  352 SKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDI 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   589 KVHLAEQSKDesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissNVRLMVSIED 668
Cdd:PRK11107  432 LVELRALSNT------------------------------------------------------------KVQLEVQIRD 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   669 TGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKcdKCSAINHmk 748
Cdd:PRK11107  452 TGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLPLDL--NPNPIID-- 527
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   749 KPNVEHLpstfKGMKAIVVDAKPVRAAVTRYHMKRLGINVDVVTSLKTAVVAAAAFERNGSPLPTKPQLdmilvekdswi 828
Cdd:PRK11107  528 GLPTDCL----AGKRLLYVEPNSAAAQATLDILSETPLEVTYSPTLSQLPEAHYDILLLGLPVTFREPL----------- 592
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   829 stEDNDSEIRLLNSRTNgNVHhkspkLALFATNITNSEfdrAKSAGFADTVIMKPLRASMIgacLQQVLELRKTRQQHPE 908
Cdd:PRK11107  593 --TMLHERLAKAKSMTD-FLI-----LALPCHEQVLAE---QLKQDGADACLSKPLSHTRL---LPALLEPCHHKQPPLL 658
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   909 GSSPATLKSLltgkKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQI 988
Cdd:PRK11107  659 PPTDESRLPL----TVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAK-QRPFDLILMDIQMPGMDGIRACELI 733
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18379305   989 RmmeketkeKTNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLyKSVAKSFKPNP 1052
Cdd:PRK11107  734 R--------QLPHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAML-KQVLLRYKPGP 788
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
440-1046 2.45e-73

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: 262.79  E-value: 2.45e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    440 KVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAGKLELE 519
Cdd:TIGR02956  454 RAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSIS 533
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    520 SVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFVKVHLAEQSKde 599
Cdd:TIGR02956  534 PRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSLNDDSS-- 611
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    600 sepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrLMVSIEDTGIGIPLVAQG 679
Cdd:TIGR02956  612 --------------------------------------------------------------LLFEVEDTGCGIAEEEQA 629
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    680 RVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKCDKcsainhmkkpnvehlpstf 759
Cdd:TIGR02956  630 TLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTRGKP------------------- 688
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    760 kgmkaivvdakpvraavtryhmkrlginvdvvtslktavVAAAAFerngsplptkpqldmilvekdswistedndseirl 839
Cdd:TIGR02956  689 ---------------------------------------AEDSAT----------------------------------- 694
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    840 lnsrtngnvhhkspklalfatnitnsefdraksagfaDTVIMKPlrasmigaclqqvlelrktrqqhpegsspatlksll 919
Cdd:TIGR02956  695 -------------------------------------LTVIDLP------------------------------------ 701
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    920 tGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKEkt 999
Cdd:TIGR02956  702 -PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFH-QHAFDLALLDINLPDGDGVTLLQQLRAIYGAKNE-- 777
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*..
gi 18379305   1000 nlewhLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:TIGR02956  778 -----VKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAV 819
PRK15347 PRK15347
two component system sensor kinase;
428-1034 1.17e-66

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 242.24  E-value: 1.17e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   428 KVEDDFHEMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLD 507
Cdd:PRK15347  376 KVAERTQALAEAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLD 455
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   508 RAKIEAGKLEL--ESVPfdIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGH 585
Cdd:PRK15347  456 FSRIESGQMTLslEETA--LLPLLDQAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLRQILVNLLGNAVKFTETGG 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   586 IFVKVhlaeQSKDEsepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVS 665
Cdd:PRK15347  534 IRLRV----KRHEQ-------------------------------------------------------------QLCFT 548
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   666 IEDTGIGIPLVAQGRVFMPFMQADSstsrNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEkcdkcsain 745
Cdd:PRK15347  549 VEDTGCGIDIQQQQQIFTPFYQADT----HSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPLN--------- 615
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   746 hmkkpnvEHLPStfkgmkaivvdakpvraavtryhmkrlginvdvvTSLKTAVVAaaaferngsPLPTKPQLDMilvekd 825
Cdd:PRK15347  616 -------EYAPP----------------------------------EPLKGELSA---------PLALHRQLSA------ 639
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   826 sW-ISTEDNDSEIRLLNsrtngnvhhksPKLALFatnitnsefdraksagfadtvimkPLRasmigacLQQVL-ELRKTR 903
Cdd:PRK15347  640 -WgITCQPGHQNPALLD-----------PELAYL------------------------PGR-------LYDLLqQIIQGA 676
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   904 QQHPEGSSPATLKSLltgkKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFE 983
Cdd:PRK15347  677 PNEPVINLPLQPWQL----QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGR-QHRFDLVLMDIRMPGLDGLE 751
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18379305   984 ATRQIRMMEKetkektNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:PRK15347  752 TTQLWRDDPN------NLDPDCMIVALTANAAPEEIHRCKKAGMNHYLTKP 796
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
433-732 5.82e-64

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 219.78  E-value: 5.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  433 FHEMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDtELSSTQRDYAQTAQVCGKALIALINEVLDRAKIE 512
Cdd:COG0642   93 LLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLE-ELDEEQREYLETILRSADRLLRLINDLLDLSRLE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  513 AGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPeIVKGDSGRFRQIIINLVGNSVKFTEKGHIfVKVHL 592
Cdd:COG0642  172 AGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGGT-VTVSV 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  593 AEQSKdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIG 672
Cdd:COG0642  250 RREGD---------------------------------------------------------------RVRISVEDTGPG 266
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  673 IPLVAQGRVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG0642  267 IPPEDLERIFEPFFRTDP--SRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
435-732 3.71e-56

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 194.36  E-value: 3.71e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  435 EMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTE--LSSTQRDYAQTAQVCGKALIALINEVLDRAKIE 512
Cdd:COG2205    1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  513 AGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEiVKGDSGRFRQIIINLVGNSVKFT-EKGHIFVKVH 591
Cdd:COG2205   81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPL-VYADPELLEQVLANLLDNAIKYSpPGGTITISAR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  592 LAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGI 671
Cdd:COG2205  160 REGD-----------------------------------------------------------------GVRISVSDNGP 174
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18379305  672 GIPLVAQGRVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG2205  175 GIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
414-732 6.64e-54

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 193.23  E-value: 6.64e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  414 LVGYILYGAAMHIVKVEDDFHEMQELkvraeaaDVAKSQFLATVSHEIRTPMNGILGMLAMLLD--TELSSTQRDYAQTA 491
Cdd:COG5002  136 LRLSALLLGLLLLAAVERDITELERL-------EQMRREFVANVSHELRTPLTSIRGYLELLLDgaADDPEERREYLEII 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  492 QVCGKALIALINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPeIVKGDSGRFRQIII 571
Cdd:COG5002  209 LEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPL-LVLGDPDRLEQVLT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  572 NLVGNSVKFT-EKGHIFVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqs 650
Cdd:COG5002  288 NLLDNAIKYTpEGGTITVSLREEDD------------------------------------------------------- 312
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  651 lsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFW 730
Cdd:COG5002  313 ----------QVRISVRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFT 382

                 ..
gi 18379305  731 FT 732
Cdd:COG5002  383 IT 384
CHASE pfam03924
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ...
177-359 5.17e-50

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: 174.79  E-value: 5.17e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    177 SAIDQETFAEYTARTAFERPLLSGVAYAEKVVNFEREMFERQH------NWVIKtmdrgePSPVRDEYAPVIFSQDSVSY 250
Cdd:pfam03924    1 DSVDREEFRRYAASLLLRRPGIQGLGWAPRVPAAERAAFEAAVraegfpDFTIR------PAGDRDEYFPIIYIEPLAGN 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    251 --LESLDMMSGEEDRENILRARETGKAVLTSPFRLL--ETHHLGVVLTFPVYKSSLPEnpTVEERIAATAGYLGGAFDVE 326
Cdd:pfam03924   75 nrALGFDMASEPVRREAIERARDTGEPVLSGPVTLVqdGDGQPGFLLYLPVYRGGPPD--TVAERRAALLGFVYAPFRID 152
                          170       180       190
                   ....*....|....*....|....*....|...
gi 18379305    327 SLVENLLGQLaGNQAIVVHVYDITNASDPLVMY 359
Cdd:pfam03924  153 DLLEAALLRL-GEDGLDLALYDGTSASAPELLY 184
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
566-735 6.38e-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: 163.05  E-value: 6.38e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  566 FRQIIINLVGNSVKFTEKGHIFVKVHLAEQSKDEsepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlv 645
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDG---------------------------------------------- 34
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  646 seeqslsefdissnVRLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHI 725
Cdd:cd16922   35 --------------VQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAISKKLVELMGGDISVESEPGQ 100
                        170
                 ....*....|
gi 18379305  726 GSTFWFTAVL 735
Cdd:cd16922  101 GSTFTFTLPL 110
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
427-1034 2.95e-45

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 177.09  E-value: 2.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   427 VKVEDDFHEMQElkvRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVL 506
Cdd:PRK10841  427 VKMEESLQEMAQ---AAEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDIL 503
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   507 DRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHI 586
Cdd:PRK10841  504 DFSKIESEQLKIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCI 583
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   587 FVKVHLAEqskdesepknalnggvseemivvskqssyntlsGYeaadgrnswdsfkhlvseeqslsefdissnvrLMVSI 666
Cdd:PRK10841  584 VLHVRVDG---------------------------------DY--------------------------------LSFRV 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   667 EDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKCDKcsainh 746
Cdd:PRK10841  599 RDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPLYGAQY------ 672
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   747 MKKPNVEHLPStfkgmKAIVVDakpVR-AAVTRYhmkrlginvdVVTSLKTAVVAAAAFERngsplpTKPQLDMILvekd 825
Cdd:PRK10841  673 PQKKGVEGLQG-----KRCWLA---VRnASLEQF----------LETLLQRSGIQVQRYEG------QEPTPEDVL---- 724
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   826 swISTEDNDSEIRL-----LNSRTNGNVHHKSPKLALFATNiTNSEFdraksagfaDTVIMKPLRASMIGACLQQVLelr 900
Cdd:PRK10841  725 --ITDDPVQKKWQGravitFCRRHIGIPLEIAPGEWVHSTA-TPHEL---------PALLARIYRIELESDDSANAL--- 789
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   901 ktrqqhpegSSPATLKSLLTGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMD 980
Cdd:PRK10841  790 ---------PSTDKAVSDNDDMMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHI-DIVLTDVNMPNMD 859
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18379305   981 GFEATRQIRmmeketkektNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:PRK10841  860 GYRLTQRLR----------QLGLTLPVIGVTANALAEEKQRCLEAGMDSCLSKP 903
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
435-802 3.87e-44

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 173.55  E-value: 3.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   435 EMQELKV-----RAEA--ADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLD 507
Cdd:PRK11466  422 ELQELVIehrqaRAEAekASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILD 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   508 RAKIEAG--KLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGH 585
Cdd:PRK11466  502 YSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGS 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   586 IFVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnSWdsfkhlvseeqslsefdissnvrlMVS 665
Cdd:PRK11466  582 IVLRSRTDGE-----------------------------------------QW------------------------LVE 596
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   666 IEDTGIGIPLVAQGRVFMPFMQAdsstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKCDKCSain 745
Cdd:PRK11466  597 VEDSGCGIDPAKLAEIFQPFVQV----SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPLRVATAPV--- 669
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 18379305   746 hmkkPNVEHLPSTFKGMKAIVVDAKPVRAAVTRYHMKRLGINVDVVTSLKTAVVAAA 802
Cdd:PRK11466  670 ----PKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETLQ 722
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
924-1044 1.81e-43

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: 153.39  E-value: 1.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnlew 1003
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLK-EEPFDLVLMDLQMPVMDGLEATRRIRELEGGGR------- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18379305 1004 HLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:cd17546   73 RTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
438-1052 4.84e-40

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 159.72  E-value: 4.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   438 ELKVRAEAADVA---KSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAG 514
Cdd:PRK11091  268 ERKRYQDALEKAsrdKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERR 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   515 KLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFVKVhlae 594
Cdd:PRK11091  348 KLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV---- 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   595 qskdesepknalnggvseemivvskqssyntlsGYEAADgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIGIP 674
Cdd:PRK11091  424 ---------------------------------RYEEGD---------------------------MLTFEVEDSGIGIP 443
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   675 LVAQGRVFMPFMQA-DSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTavlekcdkcsainhmkkpnve 753
Cdd:PRK11091  444 EDELDKIFAMYYQVkDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLT--------------------- 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   754 hlpstfkgmkaivvdakpvraavtryhmkrlgINVDVVtslktAVVAAAAFERNGSPLPTkpqLDMILVEkdswistedn 833
Cdd:PRK11091  503 --------------------------------IHAPAV-----AEEVEDAFDEDDMPLPA---LNILLVE---------- 532
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   834 dsEIRLlnsrtngnvhhkspklalfatNITnsefdraksagfadtvimkplrasmigaclqqvlelrktrqqhpegsspa 913
Cdd:PRK11091  533 --DIEL---------------------NVI-------------------------------------------------- 539
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   914 tlkslltgkkilvvddnivnrrVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmEK 993
Cdd:PRK11091  540 ----------------------VARSVLEKLGNSVDVAMTGKEALEMFD-PDEYDLVLLDIQLPDMTGLDIARELR--ER 594
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18379305   994 ETKEKTNlewhlPILAMTADVIHATyEECLKSGMDGYVSKPFEEENLYKSVAKSFKPNP 1052
Cdd:PRK11091  595 YPREDLP-----PLVALTANVLKDK-KEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQD 647
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
919-1046 2.63e-38

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 139.22  E-value: 2.63e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  919 LTGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETkek 998
Cdd:COG0784    3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRA-GPPDLILLDINMPGMDGLELLRRIRALPRLP--- 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18379305  999 tnlewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:COG0784   79 -----DIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRR 121
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
178-732 1.06e-33

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 136.84  E-value: 1.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  178 AIDQETFAEYTARTAFERPLLSGVAYAEKVVNFEREMFERQHNWVIKTMDRGEPSPVRDEYAPVIFSQDSVSYLESLDMM 257
Cdd:COG4251    5 ALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALLLLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  258 SGEEDRENILRARETGKAVLTSPFRLLETHHLGVVLTFPVYKSSLPENPTVEERIAATAGYLGGAFDVESLVENLLGQLA 337
Cdd:COG4251   85 LLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLLLLL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  338 GNQAIVVHVYDITNASDPLVMYGNQDEEADRSLSHESKLDFGDPFRKHKMICRYHQKAPIPLNVLTTVPLFFAIGFLVGY 417
Cdd:COG4251  165 ALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILL 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  418 ILYGAAMHIVKVEDDFHEMQELKVRAEAADVAKS-----QFLATVSHEIRTPMNGILGMLAMLLD---TELSSTQRDYAQ 489
Cdd:COG4251  245 LLLLILVLELLELRLELEELEEELEERTAELERSneeleQFAYVASHDLREPLRKISGFSQLLEEdygDKLDEEGREYLE 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  490 TAQVCGKALIALINEVLDRAKIeaGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVfvsDKVPEiVKGDSGRFRQI 569
Cdd:COG4251  325 RIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIEV---GPLPT-VRGDPTLLRQV 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  570 IINLVGNSVKFTEKGHIfVKVHL-AEQSKDESEpknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvsee 648
Cdd:COG4251  399 FQNLISNAIKYSRPGEP-PRIEIgAEREGGEWV----------------------------------------------- 430
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  649 qslsefdissnvrlmVSIEDTGIGIPLVAQGRVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGST 728
Cdd:COG4251  431 ---------------FSVRDNGIGIDPEYAEKIFEIFQRLHS--RDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGAT 493

                 ....
gi 18379305  729 FWFT 732
Cdd:COG4251  494 FYFT 497
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
435-732 6.95e-33

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: 133.95  E-value: 6.95e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  435 EMQELKVRAEAADVAkSQFLATVSHEIRTPMNGILGMLAMLLDTELSStQRDYAQTAQVCGKALIALINEVLDRAKIEAG 514
Cdd:COG5809  256 KLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLKGFIQLLKDTIDEE-QKTYLDIMLSELDRIESIISEFLVLAKPQAI 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  515 KLElesvPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIvKGDSGRFRQIIINLVGNSVKFTEK-GHIFVKVHLA 593
Cdd:COG5809  334 KYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPDI-LGDENQLKQVFINLLKNAIEAMPEgGNITIETKAE 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  594 EQSKdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrLMVSIEDTGIGI 673
Cdd:COG5809  409 DDDK----------------------------------------------------------------VVISVTDEGCGI 424
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18379305  674 PLVAQGRVFMPFMqadsstSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG5809  425 PEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
923-1044 9.52e-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: 122.32  E-value: 9.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEkETKektnle 1002
Cdd:COG3706    3 RILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQE-HRPDLILLDLEMPDMDGLELCRRLRADP-RTA------ 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1003 wHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:COG3706   75 -DIPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
CHASE1 COG3614
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
100-380 1.59e-31

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


Pssm-ID: 442832 [Multi-domain]  Cd Length: 588  Bit Score: 131.35  E-value: 1.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  100 HRALLPKALILWIIIVG--FISSGIYQWMDDANKIRREEVLVSMCDQRARMLQDQFSvsvNHVHALAILVSTFHyhkNPS 177
Cdd:COG3614    4 SRSLLRRRLLPLLVLLLglLLTALAWWAVRRAEEQRARARFERLADELASALEERLD---AYEQVLRGLAGLFA---ASD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  178 AIDQETFAEYTARTAFER--PLLSGVAYAEKVVNFEREMFE---RQHNW---VIKtmdrgePSPVRDEYAPVIfsqdsvs 249
Cdd:COG3614   78 DVTRAEFRRYVASLDLLRryPGIQGLGWAPRVPAAERAAFEaaaRAEGFpdfRIR------PAGERDEYFPIT------- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  250 YLES----------LDMMSGEEDRENILRARETGKAVLTSPFRLL--ETHHLGVVLTFPVYKSSLPeNPTVEERIAATAG 317
Cdd:COG3614  145 YIEPldarnrralgFDMASEPVRRAAMERARDTGRPAASGPVTLVqeTDGQPGFLLYLPVYRGGAP-PDTVAERRAALRG 223
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305  318 YLGGAFDVESLVENLLGQLAgNQAIVVHVYDITNASDPLVMY---GNQDEEADRSLSHESKLDFGD 380
Cdd:COG3614  224 FVYAPFRMDDLLAGVLGRLA-DRDLDLRLYDGTDPGPPQLLYdssPAAPAAAAPALSATRTLEVAG 288
CHASE smart01079
This domain is found in the extracellular portion of receptor-like proteins - such as serine ...
177-348 8.42e-31

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: 119.36  E-value: 8.42e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     177 SAIDQETFAEYTARTAFER--PLLSGVAYAEKVVNFEREMFERQ------HNWVIktmdRGEPSPVRDEYAPVIFSQDSV 248
Cdd:smart01079    2 ESVSRAEFRRFALELQLNRrlPGIQGLGWAPRVPPAERAAFEAAlraggpGLFNI----RLAPDGERDEYFVITYIEPLA 77
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     249 SYLESL--DMMSGEEDRENILRARETGKAVLTSPFRLLETHH--LGVVLTFPVYKSslpeNPTVEERIAATAGYLGGAFD 324
Cdd:smart01079   78 GNEAALglDLLSEPVRRAALERARDSGRPVLSGPVTLVQGTGdgRGFLLRLPVYRG----GPPTSTRREALWGFVSAVFR 153
                           170       180
                    ....*....|....*....|....
gi 18379305     325 VESLVENLLGQLAGNQaIVVHVYD 348
Cdd:smart01079  154 LDDLLEGLLGALDLPG-LDLALYD 176
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
426-792 1.08e-29

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 127.93  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   426 IVKVEDDFHEMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYA-QTAQVCGKALIALINE 504
Cdd:PRK09959  688 ITETRDLIHALEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRVEAiSLAYATGQSLLGLIGE 767
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   505 VLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAvfVSDKVPE--IVKGDSGRFRQIIINLVGNSVKFTE 582
Cdd:PRK09959  768 ILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALS--CSSTFPDhyLVKIDPQAFKQVLSNLLSNALKFTT 845
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   583 KGHIFVKVHLAEQSKDESEPKnalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrl 662
Cdd:PRK09959  846 EGAVKITTSLGHIDDNHAVIK----------------------------------------------------------- 866
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   663 mVSIEDTGIGIPLVAQGRVFMPFMQadSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEKCDKCS 742
Cdd:PRK09959  867 -MTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPVEISQQVA 943
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 18379305   743 AINHMKKPNVEhLPstfKGMKAIVVDAKPVRAAVTRYHMKRLGINVDVVT 792
Cdd:PRK09959  944 TVEAKAEQPIT-LP---EKLSILIADDHPTNRLLLKRQLNLLGYDVDEAT 989
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
433-732 3.48e-27

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: 115.83  E-value: 3.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  433 FHEMQELkVRAE--AA--DVAKSqflatVSHEIR---TPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGK---ALIALI 502
Cdd:COG5000  186 FDDITEL-LRAErlAAwgELARR-----IAHEIKnplTPIQLSAERLRRKLADKLEEDREDLERALDTIIRqvdRLKRIV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  503 NEVLDRAKIEAGKLElesvPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIvKGDSGRFRQIIINLVGNSVKFTE 582
Cdd:COG5000  260 DEFLDFARLPEPQLE----PVDLNELLREVLALYEPALKEKDIRLELDLDPDLPEV-LADRDQLEQVLINLLKNAIEAIE 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  583 -KGHIFVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvR 661
Cdd:COG5000  335 eGGEIEVSTRREDG-----------------------------------------------------------------R 349
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18379305  662 LMVSIEDTGIGIPLVAQGRVFMPFMqadssTSRNyGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG5000  350 VRIEVSDNGPGIPEEVLERIFEPFF-----TTKP-KGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
924-1045 1.29e-26

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


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 104.93  E-value: 1.29e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmeketkektNLEW 1003
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLK-EERPDLILLDINMPGMDGLELLKRIR----------RRDP 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 18379305   1004 HLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVA 1045
Cdd:pfam00072   70 TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
922-1040 1.11e-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: 105.81  E-value: 1.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKetkektnl 1001
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEE-ERPDLILLDLMLPGMDGLEVCRRLRARPS-------- 72
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:COG0745   73 --DIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEEL 109
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
452-732 2.80e-25

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 108.73  E-value: 2.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  452 QFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAqvcgkalIALINEVLDRAK--IE-----AGKLELESVPFD 524
Cdd:COG4191  144 ELAAGIAHEINNPLAAILGNAELLRRRLEDEPDPEELREA-------LERILEGAERAAeiVRslrafSRRDEEEREPVD 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  525 IRSILDDVLSLFSEESRNKSIELAVFVSDKVPEiVKGDSGRFRQIIINLVGNS---VKFTEKGHIFVKVHLAEQskdese 601
Cdd:COG4191  217 LNELIDEALELLRPRLKARGIEVELDLPPDLPP-VLGDPGQLEQVLLNLLINAidaMEEGEGGRITISTRREGD------ 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  602 pknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRV 681
Cdd:COG4191  290 -----------------------------------------------------------YVVISVRDNGPGIPPEVLERI 310
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18379305  682 FMPFMqadsSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:COG4191  311 FEPFF----TTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
922-1046 4.21e-25

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: 104.86  E-value: 4.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEkETKektnl 1001
Cdd:COG3437    7 PTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLL-EAPPDLILLDVRMPGMDGFELLRLLRADP-STR----- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:COG3437   80 --DIPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARVRN 122
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
923-1040 6.21e-25

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: 100.55  E-value: 6.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQ-IPHTFDACFMDIQMPQMDGFEATRQIRmmeketKEKTNL 1001
Cdd:cd19933    2 KVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLAsAEHSFQLVLLDLCMPEMDGFEVALRIR------KLFGRR 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1002 EWHLpILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd19933   76 ERPL-IVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
376-729 8.57e-25

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 107.24  E-value: 8.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  376 LDFGDPFRKHKMICRYHQKAPIPLNVlTTVPLFFAIGFlVGYILygaamhIVKVEDDFHEMQELKVRAEAADVAKsQFLA 455
Cdd:COG3852   70 LAEGQPVTEREVTLRRKDGEERPVDV-SVSPLRDAEGE-GGVLL------VLRDITERKRLERELRRAEKLAAVG-ELAA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  456 TVSHEIRTPMNGILGMlAMLLDTELSSTQ-RDYAQTAQVCGKALIALINEVLDRAKIEAGKLElesvPFDIRSILDDVLS 534
Cdd:COG3852  141 GLAHEIRNPLTGIRGA-AQLLERELPDDElREYTQLIIEEADRLNNLVDRLLSFSRPRPPERE----PVNLHEVLERVLE 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  535 LFSEESRnKSIELAVFVSDKVPEiVKGDSGRFRQIIINLVGNSVK-FTEKGHIFVKVHLAEQSkdesepknALNGGVSEE 613
Cdd:COG3852  216 LLRAEAP-KNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEaMPEGGTITIRTRVERQV--------TLGGLRPRL 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  614 MIVvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrlmVSIEDTGIGIPLVAQGRVFMPFMqadssTS 693
Cdd:COG3852  286 YVR-----------------------------------------------IEVIDNGPGIPEEILDRIFEPFF-----TT 313
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 18379305  694 RNyGGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:COG3852  314 KE-KGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTF 348
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
923-1046 3.41e-24

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: 98.38  E-value: 3.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEkETKektnle 1002
Cdd:cd17548    1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIAR-KEKPDLILMDIQLPGMDGLEATRLLKEDP-ATR------ 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18379305 1003 wHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17548   73 -DIPVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
925-1034 1.52e-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: 95.76  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  925 LVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKetkektnlewH 1004
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLRE-ERPDLVLLDLMMPGMDGLELLRKLRELPP----------D 69
                         90       100       110
                 ....*....|....*....|....*....|
gi 18379305 1005 LPILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:cd00156   70 IPVIVLTAKADEEDAVRALELGADDYLVKP 99
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
561-732 3.44e-23

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 95.41  E-value: 3.44e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     561 GDSGRFRQIIINLVGNSVKFT-EKGHIFVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswd 639
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTLERDGD-------------------------------------------- 36
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305     640 sfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSsTSRNYGGTGIGLSISKCLVELMRGQINF 719
Cdd:smart00387   37 ---------------------HVEITVEDNGPGIPPEDLEKIFEPFFRTDK-RSRKIGGTGLGLSIVKKLVELHGGEISV 94
                           170
                    ....*....|...
gi 18379305     720 ISRPHIGSTFWFT 732
Cdd:smart00387   95 ESEPGGGTTFTIT 107
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
447-732 1.01e-22

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: 100.75  E-value: 1.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    447 DVAKSQFLATVSHEIRTPMNGILGMLAMLLDT--ELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAGKLELESVPFD 524
Cdd:TIGR02966  111 EQMRRDFVANVSHELRTPLTVLRGYLETLADGpdEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVD 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    525 IRSILDDVLSLFSEESRNKSIELAVFVSDKVPeiVKGDSGRFRQIIINLVGNSVKFT-EKGHIfvkvhlaeqskdesepk 603
Cdd:TIGR02966  191 MPALLDHLRDEAEALSQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTpEGGTI----------------- 251
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    604 nalnggvseemivvskqssynTLSGYEAADGrnswdsfkhlvseeqslsefdissnVRLmvSIEDTGIGIPLVAQGRVFM 683
Cdd:TIGR02966  252 ---------------------TVRWRRDGGG-------------------------AEF--SVTDTGIGIAPEHLPRLTE 283
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 18379305    684 PFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:TIGR02966  284 RFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
920-1046 6.47e-21

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: 96.57  E-value: 6.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  920 TGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKetkekt 999
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLRE-EPPDLVLLDLRMPGMDGLELLRELRALDP------ 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18379305 1000 nlewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:COG2204   74 ----DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
449-514 2.70e-20

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 85.34  E-value: 2.70e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305    449 AKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAG 514
Cdd:pfam00512    1 AKSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
449-514 2.81e-20

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 85.31  E-value: 2.81e-20
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305     449 AKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAG 514
Cdd:smart00388    1 AKREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
923-1035 5.48e-20

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: 86.01  E-value: 5.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmekeTKEKTnle 1002
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAE-EELPDLILLDVMMPGMDGFEVCRRLK-----EDPET--- 71
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18379305 1003 WHLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPF 1035
Cdd:cd17538   72 RHIPVIMITAlddreDRIRG-----LEAGADDFLSKPI 104
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
561-732 5.30e-19

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: 83.19  E-value: 5.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    561 GDSGRFRQIIINLVGNSVKFTEK-GHIFVKVHLAEqskdesepknalnggvseemivvskqssyntlsgyeaadgrnswd 639
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITVTLSEGG--------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    640 sfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSstsRNYGGTGIGLSISKCLVELMRGQINF 719
Cdd:pfam02518   36 ---------------------ELTLTVEDNGIGIPPEDLPRIFEPFSTADK---RGGGGTGLGLSIVRKLVELLGGTITV 91
                          170
                   ....*....|...
gi 18379305    720 ISRPHIGSTFWFT 732
Cdd:pfam02518   92 ESEPGGGTTVTLT 104
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
924-1044 1.33e-18

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 82.12  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEketkektNLEw 1003
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQ-RFRPDVILSDIGMPGMDGYELARRLRELP-------WLA- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 18379305 1004 HLPILAMTAdviHATYEE---CLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:cd17580   72 NTPAIALTG---YGQPEDrerALEAGFDAHLVKPVDPDELIELI 112
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
924-1035 8.62e-17

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: 76.78  E-value: 8.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRmmekeTKEKTNlew 1003
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQA-EPPDLILLDVMMPGMDGFEVCRRLK-----ADPATR--- 71
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1004 HLPILAMTA--DVIHATyeECLKSGMDGYVSKPF 1035
Cdd:cd19920   72 HIPVIFLTAltDTEDKV--KGFELGAVDYITKPF 103
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
918-1040 1.29e-16

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 83.74  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   918 LLTGKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMMEKETke 997
Cdd:PRK11361    1 MTAINRILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHP-DVVLMDIRMPEMDGIKALKEMRSHETRT-- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18379305   998 ktnlewhlPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:PRK11361   78 --------PVILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
922-1046 1.91e-16

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 76.19  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPhTFDACFMDIQMPQMDGFEATRQIRMME--KETkekt 999
Cdd:cd17562    1 KKILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSK-KFDLIITDQNMPNMDGIELIKELRKLPayKFT---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18379305 1000 nlewhlPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17562   76 ------PILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
925-1034 5.40e-16

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: 74.37  E-value: 5.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  925 LVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnlewh 1004
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELARE-EQPDLIILDVMLPGMDGFEVCRRLREKGSDI--------- 70
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18379305 1005 lPILAMTA-----DVIhatyeECLKSGMDGYVSKP 1034
Cdd:cd17574   71 -PIIMLTAkdeeeDKV-----LGLELGADDYITKP 99
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
923-1036 6.57e-16

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: 74.79  E-value: 6.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFG-AEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnl 1001
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLRSAGyLEVVSFTDPREALAWCR-ENPPDLILLDYMMPGMDGLEFIRRLRALPGLE------ 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPFE 1036
Cdd:cd17551   75 --DVPIVMITADTDREVRLRALEAGATDFLTKPFD 107
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
923-1034 6.72e-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: 74.42  E-value: 6.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKF-GAEVVC-AESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektn 1000
Cdd:COG4753    1 KVLIVDDEPLIREGLKRILEWEaGFEVVGeAENGEEALELLEE-HKPDLVITDINMPGMDGLELLEAIRELDPDTK---- 75
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1001 lewhlpILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:COG4753   76 ------IIILSGYSDFEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
919-1046 7.37e-16

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 75.39  E-value: 7.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  919 LTGKKILVVDDNIVNRRVAAGALKKF-GAEVV-CAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRmmeketk 996
Cdd:COG4565    1 MKMIRVLIVEDDPMVAELLRRYLERLpGFEVVgVASSGEEALALLAE-HRPDLILLDIYLPDGDGLELLRELR------- 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 18379305  997 ektNLEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:COG4565   73 ---ARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALER 119
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
449-510 1.26e-15

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: 72.25  E-value: 1.26e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305  449 AKSQFLATVSHEIRTPMNGILGMLAMLLDTELSS-TQRDYAQTAQVCGKALIALINEVLDRAK 510
Cdd:cd00082    3 AKGEFLANVSHELRTPLTAIRGALELLEEELLDDeEQREYLERIREEAERLLRLINDLLDLSR 65
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
922-1046 1.34e-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: 74.06  E-value: 1.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKEtkektnl 1001
Cdd:COG5803    3 KKILIVDDQAGIRMLLKEVLKKEGYEVFQAANGKEALEKVK-ELKPDLVLLDMKMPGMDGIEILKEIKEIDPD------- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1002 ewhLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:COG5803   75 ---IPVIMMTAYGELDMVEEAKELGAKGYFTKPFDIDELREAVNK 116
PRK09303 PRK09303
histidine kinase;
449-732 2.48e-15

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 79.22  E-value: 2.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   449 AKSQFLATVSHEIRTPmngiLGMLAMLLDT-ELSSTQRDYAQTAQVCGKaLI-----------ALINEVLDRAKIEAGKL 516
Cdd:PRK09303  150 FKDRVLAMLAHDLRTP----LTAASLALETlELGQIDEDTELKPALIEQ-LQdqarrqleeieRLITDLLEVGRTRWEAL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   517 ELESVPFDIRSILDDVLSLFSEESRNKSIElavFVSDkVPE---IVKGDSGRFRQIIINLVGNSVKFTEK-GHIFVKV-H 591
Cdd:PRK09303  225 RFNPQKLDLGSLCQEVILELEKRWLAKSLE---IQTD-IPSdlpSVYADQERIRQVLLNLLDNAIKYTPEgGTITLSMlH 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   592 LAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGI 671
Cdd:PRK09303  301 RTTQ-----------------------------------------------------------------KVQVSICDTGP 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305   672 GIPLVAQGRVFMPF--MQADSSTSrnygGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:PRK09303  316 GIPEEEQERIFEDRvrLPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFT 374
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
922-1048 2.80e-15

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: 73.08  E-value: 2.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVC-AESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektn 1000
Cdd:cd17542    1 KKVLIVDDAAFMRMMLKDILTKAGYEVVGeAANGEEAVEKYK-ELKPDLVTMDITMPEMDGIEALKEIKKIDPNAK---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18379305 1001 lewhlpILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAKSF 1048
Cdd:cd17542   76 ------VIMCSAMGQEEMVKEAIKAGAKDFIVKPFQPERVLEAVEKVL 117
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
442-732 1.72e-14

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: 77.04  E-value: 1.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    442 RAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQ-RDYAQTAQVCGKALIALINEVLDRAKIEAGKLELES 520
Cdd:TIGR01386  233 RLEDAFQRLSQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEyREVLESNLEELERLSRMVSDMLFLARADNGQLALER 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    521 VPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPeivkGDSGRFRQIIINLVGNSVKFTEKGHIfVKVHLAEQSkdes 600
Cdd:TIGR01386  313 VRLDLAAELAKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGT-ITVRIERRS---- 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305    601 epknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslSEFDissnvrlmVSIEDTGIGIPLVAQGR 680
Cdd:TIGR01386  384 ---------------------------------------------------DEVR--------VSVSNPGPGIPPEHLSR 404
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 18379305    681 VFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQInFISRPHIGSTFWFT 732
Cdd:TIGR01386  405 LFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRA-SAESPDGKTRFILR 455
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
922-1046 5.97e-14

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: 69.50  E-value: 5.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGA-EVVCAESGQVALgllQIPHTF--DACFMDIQMPQMDGFEATRQIRmMEKETKek 998
Cdd:cd17552    2 KRILVIDDEEDIREVVQACLEKLAGwEVLTASSGQEGL---EKAATEqpDAILLDVMMPDMDGLATLKKLQ-ANPETQ-- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18379305  999 tnlewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17552   76 -----SIPVILLTAKAQPSDRQRFASLGVAGVIAKPFDPLTLAEQIAK 118
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
923-1042 7.77e-14

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: 68.90  E-value: 7.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAE-VVCAESGQVALGLLQIPhTFDACFMDIQMPQMDGFEATRQIRMmEKETKektnl 1001
Cdd:cd19923    2 KVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAG-GFDFVITDWNMPNMDGLELLKTIRA-DGALS----- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPFE----EENLYK 1042
Cdd:cd19923   75 --HLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTaatlKEKLEK 117
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
435-729 9.89e-14

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: 75.15  E-value: 9.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  435 EMQELKVRAEAADVAkSQFLATVSHEIRTPMNGILGMLAMLLDTElsSTQRDYAQtaqvcgkaLI--------ALINEVL 506
Cdd:COG5805  273 EAEELMARSEKLSIA-GQLAAGIAHEIRNPLTSIKGFLQLLQPGI--EDKEEYFD--------IMlseldrieSIISEFL 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  507 DRAKIEAGKLElesvPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIvKGDSGRFRQIIINLVGNSVkftekghi 586
Cdd:COG5805  342 ALAKPQAVNKE----KENINELIQDVVTLLETEAILHNIQIRLELLDEDPFI-YCDENQIKQVFINLIKNAI-------- 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  587 fvkvhlaeqskdESEPknalNGGVseemIVVskqssyntlsgyeaadgrnswdsfkHLVSEEQSlsefdissnvrLMVSI 666
Cdd:COG5805  409 ------------EAMP----NGGT----ITI-------------------------HTEEEDNS-----------VIIRV 432
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305  667 EDTGIGIPLVAQGRVFMPFMqadsSTSRNygGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:COG5805  433 IDEGIGIPEERLKKLGEPFF----TTKEK--GTGLGLMVSYKIIENHNGTIDIDSKVGKGTTF 489
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
924-1044 1.05e-13

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


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 68.31  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKK-FGAEVVC-AESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmeketkektNL 1001
Cdd:cd17535    1 VLIVDDHPLVREGLRRLLESePDIEVVGeAADGEEALALLR-ELRPDVVLMDLSMPGMDGIEALRRLR----------RR 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18379305 1002 EWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:cd17535   70 YPDLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIEAI 112
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
922-1037 1.40e-13

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: 68.02  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDD--NIvnRRVAAGALKKFGAEVVCAESGQVALGLLQIPHtFDACFMDIQMPQMDGFEATRQIRMMEKEtkekt 999
Cdd:cd17554    1 KKILVVDDeeNI--RELYKEELEDEGYEVVTAGNGEEALEKLESED-PDLVILDIKMPGMDGLETLRKIREKKPD----- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18379305 1000 nlewhLPILAMTAdviHATYEECLKS-GMDGYV--SKPFEE 1037
Cdd:cd17554   73 -----LPVIICTA---YSEYKSDFSSwAADAYVvkSSDLTE 105
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
449-732 1.87e-13

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 73.89  E-value: 1.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   449 AKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYA-QTAQVCGKALIALINEVLDRAKIEAG-KLELES---VPF 523
Cdd:PRK11006  203 ARRNFFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKAlHTMREQTQRMEGLVKQLLTLSKIEAApTIDLNEkvdVPM 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   524 DIRSILDDVLSLfSEESRNksielAVFVSDKVPEiVKGDSGRFRQIIINLVGNSVKFTEKG-HIFVkvhlaeqskdesep 602
Cdd:PRK11006  283 MLRVLEREAQTL-SQGKHT-----ITFEVDNSLK-VFGNEDQLRSAISNLVYNAVNHTPEGtHITV-------------- 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   603 knalnggvseemivvskqSSYNTLSGyeaadgrnswdsfkhlvseeqslSEFdissnvrlmvSIEDTGIGIPLVAQGRVF 682
Cdd:PRK11006  342 ------------------RWQRVPQG-----------------------AEF----------SVEDNGPGIAPEHIPRLT 370
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 18379305   683 MPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:PRK11006  371 ERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFV 420
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
921-1041 2.19e-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: 69.99  E-value: 2.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  921 GKKILVVDDNIVNRRVAAGALKKFGAEVV-CAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIrmmeketkekt 999
Cdd:COG3707    3 GLRVLVVDDEPLRRADLREGLREAGYEVVaEAADGEDAVELVR-ELKPDLVIVDIDMPDRDGLEAARQI----------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1000 NLEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLY 1041
Cdd:COG3707   71 SEERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLL 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
922-1044 2.40e-13

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: 67.43  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVV-CAESGQVALGLLQIpHTFDACFMDIQMP-QMDGFEATRQIRMmeketkekt 999
Cdd:cd17534    1 KKILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEE-NKPDLILMDINLKgDMDGIEAAREIRE--------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1000 nlEWHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:cd17534   71 --KFDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
924-1046 4.82e-13

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: 66.59  E-value: 4.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRvaagALKK------FGAEVVC-AESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETK 996
Cdd:cd17536    1 VLIVDDEPLIRE----GLKKlidweeLGFEVVGeAENGEEALELIEE-HKPDIVITDIRMPGMDGLELIEKIRELYPDIK 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18379305  997 ektnlewhlpILAMTAdviHATYE---ECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17536   76 ----------IIILSG---YDDFEyaqKAIRLGVVDYLLKPVDEEELEEALEK 115
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
923-1046 7.69e-13

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 69.07  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKF-GAEVV-CAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRmmeketkektN 1000
Cdd:COG3279    3 KILIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEE-HKPDLVFLDIQMPGLDGFELARQLR----------E 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18379305 1001 LEWHLPILAMTADVIHA--TYEEclkSGMDgYVSKPFEEENLYKSVAK 1046
Cdd:COG3279   72 LDPPPPIIFTTAYDEYAleAFEV---NAVD-YLLKPIDEERLAKALEK 115
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
427-732 1.46e-12

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 71.21  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   427 VKVEDD-------FHEM----QELKVRAEAADVAKSQFLATVSHEIRTPMNGIlGMLAMLL---DTELSSTQRDYAQTAQ 492
Cdd:NF040691  237 VKGEDDlarlarsFNQMadslQRQIRQLEELSRLQQRFVSDVSHELRTPLTTI-RMAADVIhdsRDDFDPATARSAELLH 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   493 VCGKALIALINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELaVFVSDKVPEIVKGDSGRFRQIIIN 572
Cdd:NF040691  316 TELDRFESLLSDLLEISRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGVEL-RVDAPGTPVVAEVDPRRVERVLRN 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   573 LVGNSVKFTEKGHIFVKVhlaeqskdesepknalnggvseemivvskqssyntlsgyeAADGRnswdsfkhlvseeqsls 652
Cdd:NF040691  395 LVVNAIEHGEGKPVVVTV----------------------------------------AQDDT----------------- 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   653 efdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:NF040691  418 --------AVAVTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
428-723 1.49e-12

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 71.01  E-value: 1.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   428 KVEDDFHEMQELKVRAEAAdvaKSQFLATVSHEIRTPMNGILGMLAMLLD-------TELSSTQRDYAQtaqvcgkaLIA 500
Cdd:NF012163  221 KLAQDFNQLASTLEKNEQM---RRDFMADISHELRTPLAVLRAELEAIQDgirkftpESLDSLQAEVGT--------LTK 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   501 LINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVpeIVKGDSGRFRQIIINLVGNSVKF 580
Cdd:NF012163  290 LVDDLHDLSMSDEGALAYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRY 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   581 TEKGHifvKVHLAEQSKDESepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnv 660
Cdd:NF012163  368 TDSGG---SLHISASQRPKE------------------------------------------------------------ 384
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305   661 rLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRP 723
Cdd:NF012163  385 -VTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAAHSP 446
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
924-1040 3.92e-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: 63.80  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLL-QIPHTFDACFMDIQMPQMDGFEATRQIRmmeketkektnLE 1002
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLrENKDEFDLVITDVHMPDMDGFEFLELIR-----------LE 69
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18379305 1003 WHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17584   70 MDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
923-1041 4.88e-12

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 63.69  E-value: 4.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTFDACFMDIQMPQMDGFEATRQIRmmEKETKEKtnle 1002
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPDIKLVITDYNMPEMDGFELVREIR--KKYSRDQ---- 75
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1003 whLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLY 1041
Cdd:cd17544   76 --LAIIGISASGDNALSARFIKAGANDFLTKPFLPEEFY 112
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
635-732 5.67e-12

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: 63.18  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  635 RNSWDSFKHLVSEEQSLS-EFDISSNVRLMVSIEDTGIGIPLVAQGRVFMPFMQADSStsrnygGTGIGLSISKCLVELM 713
Cdd:cd16920   10 RNGIEAMSEGGCERRELTiRTSPADDRAVTISVKDTGPGIAEEVAGQLFDPFYTTKSE------GLGMGLSICRSIIEAH 83
                         90
                 ....*....|....*....
gi 18379305  714 RGQINFISRPHIGSTFWFT 732
Cdd:cd16920   84 GGRLSVESPAGGGATFQFT 102
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
922-977 5.96e-12

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: 61.43  E-value: 5.96e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305     922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMP 977
Cdd:smart00448    1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE-EKPDLILLDIMMP 55
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
923-1040 1.26e-11

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: 62.76  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMMEKEtkektnle 1002
Cdd:cd17615    1 RVLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRP-DAVVLDIMLPDMDGLEVLRRLRADGPD-------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18379305 1003 whLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFEEENL 1040
Cdd:cd17615   72 --VPVLFLTAkdsveDRIAG-----LTAGGDDYVTKPFSLEEV 107
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
924-1040 1.32e-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: 62.73  E-value: 1.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmMEKETKektnlew 1003
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLA-EHRPTLVISDIVMPEMDGYELCRKIK-SDPDLK------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1004 HLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFEEENL 1040
Cdd:cd17598   72 DIPVILLTTlsdprDVIRG-----LECGADNFITKPYDEKYL 108
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
924-1048 2.51e-11

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 66.98  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKEtkektnlew 1003
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVR-EQVFDLVLCDVRMAEMDGIATLKEIKALNPA--------- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 18379305  1004 hLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAKSF 1048
Cdd:PRK10365   78 -IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKAL 121
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
661-729 8.19e-11

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


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 60.20  E-value: 8.19e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:cd16925   37 RFLLTVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGLGLSIVKEFVELHGGTVTVSDAPGGGALF 105
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
924-1049 9.89e-11

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: 59.82  E-value: 9.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmeketkeKTNLEw 1003
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIK-ERRPDLVLLDIWLPDMDGLELLKEIK--------EKYPD- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18379305 1004 hLPILAMTAdviHATYE---ECLKSGMDGYVSKPFEEENLYKSVAKSFK 1049
Cdd:cd17550   71 -LPVIMISG---HGTIEtavKATKLGAYDFIEKPLSLDRLLLTIERALE 115
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
457-779 1.46e-10

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 65.47  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   457 VSHEIRTPMNGILGMLAMLLDTEL--SSTQRDYAQTAQVCGKALIaLINEVLDRAKieagKLELESVPFDIRSILDDVLS 534
Cdd:PRK13837  457 IAHNFNNILGAILGYAEMALNKLArhSRAARYIDEIISAGARARL-IIDQILAFGR----KGERNTKPFDLSELVTEIAP 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   535 LFSEeSRNKSIELAvFVSDKVPEIVKGDSGRFRQIIINLVGNSVkftekghifvkvhlaeQSKDEsepknalnGGVSEEM 614
Cdd:PRK13837  532 LLRV-SLPPGVELD-FDQDQEPAVVEGNPAELQQVLMNLCSNAA----------------QAMDG--------AGRVDIS 585
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   615 IVVSKQSSYNTLSGYEAADGRNswdsfkhlvseeqslsefdissnVRLMVSieDTGIGIPLVAQGRVFMPFMqadssTSR 694
Cdd:PRK13837  586 LSRAKLRAPKVLSHGVLPPGRY-----------------------VLLRVS--DTGAGIDEAVLPHIFEPFF-----TTR 635
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   695 NyGGTGIGLSISKCLVELMRGQINFISRPHIGSTF--WFtAVLEKCdkcsainhMKKPNVEHLP-STFKGMKAIVVDAKP 771
Cdd:PRK13837  636 A-GGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFdvYL-PPSSKV--------PVAPQAFFGPgPLPRGRGETVLLVEP 705

                  ....*...
gi 18379305   772 VRAAVTRY 779
Cdd:PRK13837  706 DDATLERY 713
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
922-1040 1.64e-10

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: 59.35  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVC-AESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIrmmekeTKEKTN 1000
Cdd:cd19932    1 VRVLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKK-HKPDLVIMDVKMPRLDGIEAAKII------TSENIA 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18379305 1001 lewhlPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd19932   74 -----PIVLLTAYSQQDLVERAKEAGAMAYLVKPFSESDL 108
orf27 CHL00148
Ycf27; Reviewed
922-1035 2.22e-10

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 62.04  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRmmeKETKektnl 1001
Cdd:CHL00148    7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRK-EQPDLVILDVMMPKLDGYGVCQEIR---KESD----- 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 18379305  1002 ewhLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPF 1035
Cdd:CHL00148   78 ---VPIIMLTAlgdvsDRITG-----LELGADDYVVKPF 108
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
924-1040 2.62e-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: 58.93  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKEtkektnlew 1003
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVIS-GNRPDAVVLDVMMPRLDGLEVCRRLRAAGND--------- 70
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18379305 1004 hLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17627   71 -LPILVLTARDSVSDRVAGLDAGADDYLVKPFALEEL 106
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
922-1035 2.94e-10

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


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 58.80  E-value: 2.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmekeTKEKTNl 1001
Cdd:cd17618    1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIV-EPRPDLILLDWMLPGGSGIQFIRRLK-----RDEMTR- 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPF 1035
Cdd:cd17618   74 --DIPIIMLTARGEEEDKVRGLEAGADDYITKPF 105
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
923-1034 3.41e-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: 58.56  E-value: 3.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGA-EVV-CAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIrMMEKETkektn 1000
Cdd:cd17541    2 RVLIVDDSAVMRKLLSRILESDPDiEVVgTARDGEEALEKIKE-LKPDVITLDIEMPVMDGLEALRRI-MAERPT----- 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18379305 1001 lewhlPIL---AMTADVIHATYeECLKSGMDGYVSKP 1034
Cdd:cd17541   75 -----PVVmvsSLTEEGAEITL-EALELGAVDFIAKP 105
PRK10610 PRK10610
chemotaxis protein CheY;
923-1049 3.44e-10

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 58.83  E-value: 3.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFG-AEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnl 1001
Cdd:PRK10610    7 KFLVVDDFSTMRRIVRNLLKELGfNNVEEAEDGVDALNKLQ-AGGFGFVISDWNMPNMDGLELLKTIRADGAMSA----- 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 18379305  1002 ewhLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAKSFK 1049
Cdd:PRK10610   81 ---LPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFE 125
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
922-1047 4.30e-10

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 57.98  E-value: 4.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnl 1001
Cdd:cd17555    1 ATILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFR-SEQPDLVLCDLRMPEMDGLEVLKQITKESPDT------ 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18379305 1002 ewhlPILAMT-----ADVIHAtyeecLKSGMDGYVSKPFEE-ENLYKSVAKS 1047
Cdd:cd17555   74 ----PVIVVSgagvmSDAVEA-----LRLGAWDYLTKPIEDlAVLEHAVRRA 116
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
925-1035 5.06e-10

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 58.05  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  925 LVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnlewh 1004
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAK-DEKPDLIILDLMLPGIDGLEVCRILRSDPKTSS-------- 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 18379305 1005 LPILAMTADVihatyEEC-----LKSGMDGYVSKPF 1035
Cdd:cd19937   72 IPIIMLTAKG-----EEFdkvlgLELGADDYITKPF 102
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
661-729 5.54e-10

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


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 57.43  E-value: 5.54e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMqadssTSRNYG-GTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:cd16943   35 QVLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRF 99
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
924-1034 6.38e-10

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: 57.76  E-value: 6.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQI-PHTFDACFMDIQ---------MPQMDGFEatrqirmMEK 993
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLeDEEDSSNFNEPKvnmiitdycMPGMTGYD-------LLK 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18379305  994 ETKEKTNLEwHLPILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:cd17581   74 KVKESSALK-EIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
922-1042 6.53e-10

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 57.55  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKF-GAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektn 1000
Cdd:cd17593    1 MKVLICDDSSMARKQLARALPADwDVEITFAENGEEALEILR-EGRIDVLFLDLTMPVMDGYEVLEALPVEQLETK---- 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1001 lewhlpILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYK 1042
Cdd:cd17593   76 ------VIVVSGDVQPEAKERVLELGALAFLKKPFDPEKLAQ 111
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
924-1034 1.02e-09

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 56.62  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHtFDACFMDIQMPQMDGFEATRQIRmmeketkEKTNLEw 1003
Cdd:cd19927    1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYI-PDLIISDIIMPGVDGYSLLGKLR-------KNADFD- 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 18379305 1004 HLPIL-----AMTADVIHAtYeeclKSGMDGYVSKP 1034
Cdd:cd19927   72 TIPVIfltakGMTSDRIKG-Y----NAGCDGYLSKP 102
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
924-1040 1.04e-09

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 56.91  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnlew 1003
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGE-EEPYDLVVLDLGLPGMDGLSVLRRWRSEGRAT-------- 71
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18379305 1004 hlPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd19934   72 --PVLILTARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
435-729 1.20e-09

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 62.29  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   435 EMQELKVRAEA-ADVAKsqFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTA--QVcgKALIALINEVLDRAKI 511
Cdd:PRK11360  376 RLQRRVARQERlAALGE--LVAGVAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVlrEV--DRLNKVIDQLLEFSRP 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   512 EAGKLelesVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVkGDSGRFRQIIINLVGNSVK-FTEKGHIFVKV 590
Cdd:PRK11360  452 RESQW----QPVSLNALVEEVLQLFQTAGVQARVDFETELDNELPPIW-ADPELLKQVLLNILINAVQaISARGKIRIRT 526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   591 HlaeqskdesepknalnggvseemivvskqssyntlsgYEAADgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTG 670
Cdd:PRK11360  527 W-------------------------------------QYSDG---------------------------QVAVSIEDNG 542
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 18379305   671 IGIPLVAQGRVFMPFMQADSStsrnygGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:PRK11360  543 CGIDPELLKKIFDPFFTTKAK------GTGLGLALSQRIINAHGGDIEVESEPGVGTTF 595
PRK10604 PRK10604
sensor protein RstB; Provisional
448-731 1.42e-09

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 61.54  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   448 VAKSQFLATVSHEIRTPMNGI---LGMLAMLLDTELSSTQRDYAQtaqvcgkaLIALINEVLDRAKIEAGKLELESVPFD 524
Cdd:PRK10604  210 ASKKQLIDGIAHELRTPLVRLryrLEMSDNLSAAESQALNRDIGQ--------LEALIEELLTYARLDRPQNELHLSEPD 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   525 ----IRSILDDVLSLFSEesrnKSIELAVFVSdkvPEIVKGDSGRFRQIIINLVGNSVKFTEKGhifVKVHLAEQSkdes 600
Cdd:PRK10604  282 lpawLSTHLADIQAVTPE----KTVRLDTPHQ---GDYGALDMRLMERVLDNLLNNALRYAHSR---VRVSLLLDG---- 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   601 epknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdisSNVRLMVsiEDTGIGIPLVAQGR 680
Cdd:PRK10604  348 ---------------------------------------------------------NQACLIV--EDDGPGIPPEERER 368
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18379305   681 VFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWF 731
Cdd:PRK10604  369 VFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDESELGGARFSF 419
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
433-717 2.04e-09

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 61.33  E-value: 2.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   433 FHEMQElkvRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTE---------LSSTQRDYAQTAQvcgkaliaLIN 503
Cdd:PRK09835  248 FNHMIE---RIEDVFTRQSNFSADIAHEIRTPITNLITQTEIALSQSrsqkeledvLYSNLEELTRMAK--------MVS 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   504 EVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAvFVSDkvPEIVKGDSGRFRQIIINLVGNSVKFTEK 583
Cdd:PRK09835  317 DMLFLAQADNNQLIPEKKMLDLADEVGKVFDFFEAWAEERGVELR-FVGD--PCQVAGDPLMLRRAISNLLSNALRYTPA 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   584 GHIfVKVHLAEQskdesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdiSSNVRLM 663
Cdd:PRK09835  394 GEA-ITVRCQEV-------------------------------------------------------------DHQVQLV 411
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18379305   664 VsiEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQI 717
Cdd:PRK09835  412 V--ENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTV 463
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
661-732 3.45e-09

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


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 55.13  E-value: 3.45e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:cd16939   30 RLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHRVALWHGGHVECDDSELGGACFRLT 101
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
924-1034 4.39e-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: 55.08  E-value: 4.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIP--------HTFDACFMDIQMPQMDGFEATRQIRmmeket 995
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLakegndlsKELDLIITDIEMPKMDGYELTFELR------ 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 18379305  996 keKTNLEWHLPILAMT--ADVIHAtyEECLKSGMDGYVSKP 1034
Cdd:cd19924   75 --DDPRLANIPVILNSslSGEFSR--ARGKKVGADAYLAKF 111
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
922-1057 5.06e-09

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: 56.85  E-value: 5.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnl 1001
Cdd:COG4567    5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQ-APPDYAVLDLRLGDGSGLDLIEALRERDPDAR----- 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305 1002 ewhlpILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSVAKSFKPNPISPSS 1057
Cdd:COG4567   79 -----IVVLTGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPPEN 129
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
924-1044 7.95e-09

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: 54.35  E-value: 7.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDD--NIVNrrVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRmmeketkeKTNl 1001
Cdd:cd17614    1 ILVVDDekPISD--ILKFNLTKEGYEVVTAYDGREALEKVEEEQP-DLILLDLMLPEKDGLEVCREVR--------KTS- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18379305 1002 ewHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:cd17614   69 --NVPIIMLTAKDSEVDKVLGLELGADDYVTKPFSNRELLARV 109
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
923-1040 9.44e-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: 54.73  E-value: 9.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFG--AEVVCAESGQVALGLLQIPHTFDAC------FMDIQMPQMDGFEATRQIrmmeke 994
Cdd:cd17557    1 TILLVEDNPGDAELIQEAFKEAGvpNELHVVRDGEEALDFLRGEGEYADAprpdliLLDLNMPRMDGFEVLREI------ 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18379305  995 tKEKTNLEwHLPILAMTA-----DVihatyEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17557   75 -KADPDLR-RIPVVVLTTsdaeeDI-----ERAYELGANSYIVKPVDFEEF 118
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
924-1040 1.01e-08

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 54.03  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNivnRRVAAG---ALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmeketKEKtn 1000
Cdd:cd17624    1 ILLVEDD---ALLGDGlktGLRKAGYAVDWVRTGAEAEAALA-SGPYDLVILDLGLPDGDGLDLLRRWR------RQG-- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1001 leWHLPILAMTA-----DVIhatyeECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17624   69 --QSLPVLILTArdgvdDRV-----AGLDAGADDYLVKPFALEEL 106
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
665-731 1.18e-08

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: 53.75  E-value: 1.18e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18379305  665 SIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWF 731
Cdd:cd16952   36 SVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHVMSRHDARLLIASELGKGSRFTC 102
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
922-1036 1.28e-08

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: 53.82  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMmeketkektnl 1001
Cdd:cd19919    1 KTVWIVDDDSSIRWVLERALAGAGLTVTSFENAQEALAALAS-SQPDVLISDIRMPGMDGLALLAQIKQ----------- 68
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1002 EW-HLPILAMTAdviHATYEECLKSGMDG---YVSKPFE 1036
Cdd:cd19919   69 RHpDLPVIIMTA---HSDLDSAVSAYQGGafeYLPKPFD 104
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
656-730 1.60e-08

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: 53.56  E-value: 1.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18379305  656 ISSNVRLMVSIEDTGIGIPLVAQGRVFMPFMQADSstsRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFW 730
Cdd:cd16940   39 LSADDGAVIRVEDNGPGIDEEELEALFERFYRSDG---QNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAW 110
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
453-717 1.69e-08

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 58.11  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   453 FLATVSHEIRTPMNGILGMLAMLLD-------TELSSTQrdyaqtAQVcgKALIALINEVLDRAKIEAGKLELESVPFDI 525
Cdd:PRK10549  243 FMADISHELRTPLAVLRGELEAIQDgvrkftpESVASLQ------AEV--GTLTKLVDDLHQLSLSDEGALAYRKTPVDL 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   526 RSILDDVLSLFSEESRNKSIELAVFVSDKVPeiVKGDSGRFRQIIINLVGNSVKFTEKGhifvkvhlaeqskdesepkna 605
Cdd:PRK10549  315 VPLLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSG--------------------- 371
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   606 lnGGVseeMIVVSKQSSYNTLSGYEAADGrnswdsfkhlVSEEQslsefdissnvrlmvsiedtgigiplvaQGRVFMPF 685
Cdd:PRK10549  372 --GSL---HISAEQRDKTLRLTFADSAPG----------VSDEQ----------------------------LQKLFERF 408
                         250       260       270
                  ....*....|....*....|....*....|..
gi 18379305   686 MQADSSTSRNYGGTGIGLSISKCLVELMRGQI 717
Cdd:PRK10549  409 YRTEGSRNRASGGSGLGLAICLNIVEAHNGRI 440
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
456-726 1.92e-08

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 57.93  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   456 TVSHEIRTPMNGILGMlAMLLDTELSSTQRD-YAQTAQVCGKALIALINEVLDRAKIEAGKLELESVPFDIRSILDDVLS 534
Cdd:PRK11100  262 TLTHELKSPLAAIRGA-AELLQEDPPPEDRArFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVE 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   535 LFSEESRNKSIELAVFVSDKVpeiVKGDSGRFRQIIINLVGNSVKFT-EKGHIFVKVHLAEQskdesepknalnggvsee 613
Cdd:PRK11100  341 AREAQAAAKGITLRLRPDDAR---VLGDPFLLRQALGNLLDNAIDFSpEGGTITLSAEVDGE------------------ 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   614 mivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMqadsSTS 693
Cdd:PRK11100  400 -----------------------------------------------QVALSVEDQGPGIPDYALPRIFERFY----SLP 428
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 18379305   694 RNYGG---TGIGLSISKCLVELMRGQINFISRPHIG 726
Cdd:PRK11100  429 RPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGG 464
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
664-729 4.35e-08

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: 52.90  E-value: 4.35e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305  664 VSIEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:cd16947   55 IDIWDKGKGISETEKDHVFERLYTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVF 120
PRK10490 PRK10490
sensor protein KdpD; Provisional
439-737 4.58e-08

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 57.35  E-value: 4.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   439 LKVRAEAADVA------KSQFLATVSHEIRTPMNGILGMlAMLLDTELSSTQRDYAQTA-----QVCGKalIALINEVLD 507
Cdd:PRK10490  647 LTASEEQARLAsereqlRNALLAALSHDLRTPLTVLFGQ-AEILTLDLASEGSPHARQAseirqQVLNT--TRLVNNLLD 723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   508 RAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVfvSDKVPeIVKGDSGRFRQIIINLVGNSVKFTekghif 587
Cdd:PRK10490  724 MARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGHPINLSL--PEPLT-LIHVDGPLFERVLINLLENAVKYA------ 794
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   588 vkvhlaeqskdesepknalnggvseemivvskqssyntlsGYEAADGRNSWdsfkhlVSEEQslsefdissnvrLMVSIE 667
Cdd:PRK10490  795 ----------------------------------------GAQAEIGIDAH------VEGER------------LQLDVW 816
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   668 DTGIGIPLVAQGRVFMPFMQADSSTSrnYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFTAVLEK 737
Cdd:PRK10490  817 DNGPGIPPGQEQLIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRVTLPLET 884
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
665-732 4.67e-08

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: 51.94  E-value: 4.67e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18379305  665 SIEDTGIGIPLVAQGRVFMPFMQADSSTSrnYGGTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:cd16921   38 YVRDNGIGIDPEYAEKVFGIFQRLHSREE--YEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFT 103
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
448-729 1.09e-07

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 55.56  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   448 VAKSQFLATVSHEIRTPMNGILGmLAMLLDTELSSTQRDYaQTAQVCGKA---LIALINEVLDRAKieagKLELESVPFD 524
Cdd:PRK10364  235 VALGHLAAGVAHEIRNPLSSIKG-LAKYFAERAPAGGEAH-QLAQVMAKEadrLNRVVSELLELVK----PTHLALQAVD 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   525 IRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIvKGDSGRFRQIIINLVGNSVkftekghifvkvhlaeQSKDEsepkn 604
Cdd:PRK10364  309 LNDLINHSLQLVSQDANSREIQLRFTANDTLPEI-QADPDRLTQVLLNLYLNAI----------------QAIGQ----- 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   605 alnGGVseemIVVSKQSSyntlsgyeaadgrnswdsfkhlvseeqslsefdiSSNVRLMVSieDTGIGIPLVAQGRVFMP 684
Cdd:PRK10364  367 ---HGV----ISVTASES----------------------------------GAGVKISVT--DSGKGIAADQLEAIFTP 403
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 18379305   685 FMqadssTSRNyGGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:PRK10364  404 YF-----TTKA-EGTGLGLAVVHNIVEQHGGTIQVASQEGKGATF 442
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
924-1040 1.22e-07

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 51.23  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMMEketkektnlew 1003
Cdd:cd17619    3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDI-DLVLLDINLPGKDGLSLTRELREQS----------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1004 HLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFEEENL 1040
Cdd:cd17619   71 EVGIILVTGrddevDRIVG-----LEIGADDYVTKPFNPREL 107
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
924-1034 1.25e-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: 50.63  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQvaLGLLQI-PHTFDACFMDIQMPQMDGFEATRQIRmmeketkektnlE 1002
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQ--EGLLEAaTRKPDLIILDLGLPDMDGLEVIRRLR------------E 66
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18379305 1003 W-HLPILAMTA-----DVIHAtyeecLKSGMDGYVSKP 1034
Cdd:cd17620   67 WsAVPVIVLSArdeesDKIAA-----LDAGADDYLTKP 99
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
666-717 1.45e-07

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: 50.40  E-value: 1.45e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18379305  666 IEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQI 717
Cdd:cd16949   35 ITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAIAERAIEQHGGKI 86
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
428-717 1.69e-07

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 55.46  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  428 KVEDDFHEMQ-ELKVRAEAADVAksQFLATVSHEIRTPMNgilGMLAMLLDTELSSTQRDYAQTAQVCGKA--LIALINE 504
Cdd:COG4192  412 RIEKNLRQTQdELIQAAKMAVVG--QTMTSLAHELNQPLN---AMSMYLFSAKKALEQENYAQLPTSLDKIegLIERMDK 486
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  505 VLDRAKIEAGKLELESVPFDIRSILDDVLSLFseESRNKSIELAVFVSDKVPeiVKGDSGRFRQIIINLvgnsvkftekg 584
Cdd:COG4192  487 IIKSLRQFSRKSDTPLQPVDLRQVIEQAWELV--ESRAKPQQITLHIPDDLM--VQGDQVLLEQVLVNL----------- 551
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  585 hiFVkvhlaeqskdesepkNALNGGVSEEMIVVSKQssyntlsgyeaadgrnswdsfkhlvseeqslsefdiSSNVRLMV 664
Cdd:COG4192  552 --LV---------------NALDAVATQPQISVDLL------------------------------------SNAENLRV 578
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18379305  665 SIEDTGIGIPLVaqGRVFMPFmqadssTSRNYGGTGIGLSISKCLVELMRGQI 717
Cdd:COG4192  579 AISDNGNGWPLV--DKLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDL 623
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
923-1035 1.89e-07

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: 50.19  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTFDACFMDIQMPQMDGFEATRQIRmmeketkeKTNLE 1002
Cdd:cd18160    1 TILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKDIDIVVTDIVMPEMDGIELAREAR--------KIDPD 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 18379305 1003 whLPILAMTAdviHATYEECLKSGMDG---YVSKPF 1035
Cdd:cd18160   73 --VKILFISG---GAAAAPELLSDAVGdnaTLKKPF 103
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
924-1035 1.96e-07

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: 50.36  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESgqvalgLLQIPHTF-----DACFMDIQMPQMDGFEATRQIRMMEketkek 998
Cdd:cd18159    1 ILIVEDDETIASLLKKHLEKWGYEVVLIED------FEDVLEEFlqfkpDLVLLDINLPYFDGFYWCREIRQIS------ 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305  999 tnlewHLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPF 1035
Cdd:cd18159   69 -----NVPIIFISSrddnmDQVMA-----INMGGDDYITKPF 100
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
662-723 2.49e-07

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: 50.09  E-value: 2.49e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18379305  662 LMVSIEDTGIGIPLVAQGRVFMPFMqadssTSRNyGGTGIGLSISKCLVELMRGQINFISRP 723
Cdd:cd16918   44 LRVSVIDNGPGIPPDLQDTIFYPMV-----SGRE-NGTGLGLAIAQNIVSQHGGVIECDSQP 99
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
925-1040 2.63e-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: 2.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  925 LVVDDNIVNRRVAAGALKKFGAEVVCAESGQValGLLQIPHT-FDACFMDIQMPQMDGFEATRQIRMMEKETkektnlew 1003
Cdd:cd17625    1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEE--GLEYALSGiYDLIILDIMLPGMDGLEVLKSLREEGIET-------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18379305 1004 hlPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFEEENL 1040
Cdd:cd17625   71 --PVLLLTAldaveDRVKG-----LDLGADDYLPKPFSLAEL 105
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
923-988 3.29e-07

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 50.28  E-value: 3.29e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18379305  923 KILVVDDNIVNRRVAAGALKK-FGAEVV-CAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQI 988
Cdd:COG2197    3 RVLIVDDHPLVREGLRALLEAePDIEVVgEAADGEEALELLEE-LRPDVVLLDIRMPGMDGLEALRRL 69
pleD PRK09581
response regulator PleD; Reviewed
923-1034 3.35e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 54.14  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIrmmeketkeKTNLE 1002
Cdd:PRK09581    4 RILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICE-REQPDIILLDVMMPGMDGFEVCRRL---------KSDPA 73
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18379305  1003 W-HLPILAMTA-DVIHATYEEcLKSGMDGYVSKP 1034
Cdd:PRK09581   74 TtHIPVVMVTAlDDPEDRVRG-LEAGADDFLTKP 106
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
555-729 5.93e-07

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: 49.76  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  555 VPEIVKGDSGRFRQIIINLVGNSVKFTEK-GHIFVKVHLAEQSKDESEpknalnggvseemivvskqssyntlsgyeaad 633
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRNGgGNITFRVFLEGGSEDRSD-------------------------------- 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  634 grNSWDSFKHLVSEEqslsefdiSSNVRLMVSIEDTGIGiplvAQGRVFMPfmqadSSTSRNYG----GTGIGLSISKCL 709
Cdd:cd16938   49 --RDWGPWRPSMSDE--------SVEIRFEVEINDSGSP----SIESASMR-----NSLNRRYNlselGEHLSFSICKQL 109
                        170       180
                 ....*....|....*....|
gi 18379305  710 VELMRGQINFISRPHIGSTF 729
Cdd:cd16938  110 VQLMGGNIWIVPGSGLGTTM 129
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
924-1035 6.67e-07

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: 48.84  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLqIPHTFDACFMDIQMPQMDGFEATRQIRmmeKETKektnlew 1003
Cdd:cd17623    1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAAL-LEGSPDLVVLDVMLPKMNGLDVLKELR---KTSQ------- 69
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18379305 1004 hLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPF 1035
Cdd:cd17623   70 -VPVLMLTArgddiDRILG-----LELGADDYLPKPF 100
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
923-1040 7.15e-07

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: 49.01  E-value: 7.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRmmeketkektnLE 1002
Cdd:cd17626    2 RILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRP-DLVLLDLMLPGIDGIEVCRQIR-----------AE 69
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18379305 1003 WHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17626   70 SGVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKEL 107
PRK15479 PRK15479
transcriptional regulator TctD;
923-1040 7.21e-07

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 51.26  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRmmeketKEKTNLe 1002
Cdd:PRK15479    2 RLLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQS-EMYALAVLDINMPGMDGLEVLQRLR------KRGQTL- 73
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18379305  1003 whlPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:PRK15479   74 ---PVLLLTARSAVADRVKGLNVGADDYLPKPFELEEL 108
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
922-1034 9.59e-07

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 48.59  E-value: 9.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnl 1001
Cdd:cd17563    1 KSLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALARE-EKPDYAVLDLRLGGDSGLDLIPPLRALQPDAR----- 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 18379305 1002 ewhlpILAMT--ADVihATYEECLKSGMDGYVSKP 1034
Cdd:cd17563   75 -----IVVLTgyASI--ATAVEAIKLGADDYLAKP 102
envZ PRK09467
osmolarity sensor protein; Provisional
454-723 1.23e-06

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 52.22  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   454 LATVSHEIRTPMNGIlgMLAmlldTELSSTQRDYAQTAQV-----CGkaliALINEVLDRAKIEAgklELESVPFDIRSI 528
Cdd:PRK09467  233 MAGVSHDLRTPLTRI--RLA----TEMMSEEDGYLAESINkdieeCN----AIIEQFIDYLRTGQ---EMPMEMADLNAL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   529 LDDVLSlfSEESRNKSIELAVfvsDKVPEIVKGDSGRFRQIIINLVGNSVKFtekGHIFVKVhlaeqskdesepknalng 608
Cdd:PRK09467  300 LGEVIA--AESGYEREIETAL---QPGPIEVPMNPIAIKRALANLVVNAARY---GNGWIKV------------------ 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   609 gvseemivvskqSSYNTLSgyeaadgrnswdsfkhlvseeqslsefdissnvRLMVSIEDTGIGIPLVAQGRVFMPFMQA 688
Cdd:PRK09467  354 ------------SSGTEGK---------------------------------RAWFQVEDDGPGIPPEQLKHLFQPFTRG 388
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 18379305   689 DssTSRNYGGTGIGLSISKCLVELMRGQINFISRP 723
Cdd:PRK09467  389 D--SARGSSGTGLGLAIVKRIVDQHNGKVELGNSE 421
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
923-1035 1.57e-06

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: 47.83  E-value: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEV-VCAESGQVALGLLQIPHtfDACFMDIQMPQMDGFEATRQIRMMEKetkektnl 1001
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVtAAADGAEEARLMLHRRV--DLVLLDLRLGQESGLDLLRTIRARSD-------- 70
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1002 ewhLPILAMTADvihaTYEEC-----LKSGMDGYVSKPF 1035
Cdd:cd17594   71 ---VPIIIISGD----RRDEIdrvvgLELGADDYLAKPF 102
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
562-723 1.78e-06

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: 47.46  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  562 DSGRFRQIIINLVGNSVKFTEKGHIfVKVHLAeqskdeSEPKNalnggvseemivvskqssyntlsgyeaadgrnswdsf 641
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGK-LRIRAA------QTPQE------------------------------------- 36
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  642 khlvseeqslsefdissnVRLMVsiEDTGIGIPLVAQGRVFMPFMQADSSTSRNYGGTGIGLSISKCLVELMRGQINFIS 721
Cdd:cd16946   37 ------------------VRLDV--EDSAPGVSDDQLARLFERFYRVESSRNRASGGSGLGLAICHNIALAHGGTISAEH 96

                 ..
gi 18379305  722 RP 723
Cdd:cd16946   97 SP 98
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
924-1046 2.20e-06

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: 47.87  E-value: 2.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKEtkektnlew 1003
Cdd:cd17549    1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALS-PDFPGVVISDIRMPGMDGLELLAQIRELDPD--------- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 18379305 1004 hLPILAMTA--DVIHATyeECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17549   71 -LPVILITGhgDVPMAV--EAMRAGAYDFLEKPFDPERLLDVVRR 112
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
922-989 3.10e-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: 47.01  E-value: 3.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18379305  922 KKILVVDD--NIVN--RRVaagaLKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIR 989
Cdd:cd17569    1 PTILLVDDepNILKalKRL----LRREGYEVLTATSGEEALEILK-QEPVDVVISDQRMPGMDGAELLKRVR 67
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
661-731 3.17e-06

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: 46.68  E-value: 3.17e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMqadssTSRNYG-GTGIGLSISKCLVELMRGQINFISRPHIGSTFWF 731
Cdd:cd16976   34 RLVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTF 100
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
661-722 3.29e-06

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: 46.67  E-value: 3.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMQADSstSRNYGGTGIGLSISKCLVELMRGQINFISR 722
Cdd:cd16950   30 RTRIQVLDNGPGIAPEEVDELFQPFYRGDN--ARGTSGTGLGLAIVQRISDAHGGSLTLANR 89
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
923-1040 6.42e-06

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 48.65  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQipHTFDACFMDIQMPQMDGFEATRQIRMMEKetkektnle 1002
Cdd:PRK10955    3 KILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD--DSIDLLLLDVMMPKKNGIDTLKELRQTHQ--------- 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18379305  1003 whLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:PRK10955   72 --TPVIMLTARGSELDRVLGLELGADDYLPKPFNDREL 107
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
924-1051 6.96e-06

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: 45.99  E-value: 6.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVC--AESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKetkektnl 1001
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIVgeAENGEEALEAIEE-LKPDVVFLDIQMPGLDGLELAKKLSKLAK-------- 71
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 18379305 1002 ewhlPILamtadVIHAT-YEECLKSGMD----GYVSKPFEEENLYKSVAKSFKPN 1051
Cdd:cd17532   72 ----PPL-----IVFVTaYDEYAVEAFElnavDYLLKPFSEERLAEALAKLRKRL 117
glnL PRK11073
nitrogen regulation protein NR(II);
664-723 8.70e-06

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 49.31  E-value: 8.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   664 VSIEDTGIGIPLVAQGRVFMPFMQADSstsrnyGGTGIGLSISKCLVELMRGQINFISRP 723
Cdd:PRK11073  283 IDIEDNGPGIPPHLQDTLFYPMVSGRE------GGTGLGLSIARNLIDQHSGKIEFTSWP 336
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
661-729 8.76e-06

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 49.46  E-value: 8.76e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFmpfmqADSSTSRNYGGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:COG3290  317 ELVIEVEDSGPGIPEELLEKIF-----ERGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVF 380
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
662-731 1.26e-05

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: 45.45  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18379305  662 LMVSIEDTGIGIPLVAQGRVFMPFMqadssTSRNYG-GTGIGLSISKCLVELMRGQINFISRPHIGSTF--WF 731
Cdd:cd16919   48 VCLEVSDTGSGMPAEVLRRAFEPFF-----TTKEVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVriYL 115
fixJ PRK09390
response regulator FixJ; Provisional
926-1049 1.26e-05

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 47.30  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   926 VVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLqiPHTFDACFM-DIQMPQMDGFEATRQIrmmeKETKEKtnlewh 1004
Cdd:PRK09390    8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDAL--PGLRFGCVVtDVRMPGIDGIELLRRL----KARGSP------ 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18379305  1005 LPILAMT--ADVIHATyeECLKSGMDGYVSKPFEEENLYKSVAKSFK 1049
Cdd:PRK09390   76 LPVIVMTghGDVPLAV--EAMKLGAVDFIEKPFEDERLIGAIERALA 120
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
924-1040 1.36e-05

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: 45.28  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGllQIPHTFDACF-MDIQMPQMDGFEATRQIRmmeketkektNLE 1002
Cdd:cd17537    3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLA--AAPPDQPGCLvLDVRMPGMSGLELQDELL----------ARG 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18379305 1003 WHLPILAMT--ADVIHATyeECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17537   71 SNIPIIFITghGDVPMAV--EAMKAGAVDFLEKPFRDQVL 108
CHASE COG3452
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ...
107-574 1.69e-05

Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 442675 [Multi-domain]  Cd Length: 785  Bit Score: 49.16  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  107 ALILWIIIVGFISSGIYQwmdDANKIRREEVLVSMCDQRARmLQDQFSVSVNHVHALAILVSTfhyhkNPSaIDQETFAE 186
Cdd:COG3452   20 AFLLLLAVGAVLERLLRE---QEEQQLRAEVLQELSAIRAR-LEGELNARLSLLRGLAALVEA-----NPG-ISQEEFER 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  187 YtARTAFER-PLLSGVAYAEkvvnferemferqhNWVIKTMdrgEPspvrdeyapvifsqdsvsyLES------LDMMSG 259
Cdd:COG3452   90 L-ARNLLEDyPGIRNIALAP--------------DGVIRYV---YP-------------------LAGneaalgLDLRTD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  260 EEDRENILRARETGKAVLTSPFRLLEThHLGVVLTFPVYksslpeNPTVEERIaatAGYLGGAFDVESLVENLLGQLAGN 339
Cdd:COG3452  133 PEQRAAALRARESGQLVLAGPVNLVQG-GRGLIGRLPVF------LDGGDDRF---WGFVSAVIDLDRLLDSAGLDDAQD 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  340 Q-AIVVHVYDITNASDPLVmYGnqDEEADRSLSHESKLDFGDpfrkhkmicRYHQKAPIP----LNVLTTVPLFFAIGFL 414
Cdd:COG3452  203 GyQIALRGRDGDGAEGEVF-YG--DAALFDQDPVTLEVNLPG---------GSWQLAAAPkggwLASPRNALPLRLAGLL 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  415 VGyILYGAAMHIVKVEDDFHEMQELKVRAEAADVAKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQvc 494
Cdd:COG3452  271 IS-LLLALLVYLLRQLLLLRLLLLLLRLELIAAALLLLLLALDLLLELLLLLRLAEALLQERLRALALLAALEDLLLL-- 347
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  495 gkALIALINEVLDRAKIEAGKLELESVPFDIRSILDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLV 574
Cdd:COG3452  348 --KFDRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDGRVAVILIIEALELAEARLAALDQERDA 425
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
923-1020 1.78e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 47.95  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGA-EVV-CAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIrMMEKETkektn 1000
Cdd:PRK12555    2 RIGIVNDSPLAVEALRRALARDPDhEVVwVATDGAQAVERCA-AQPPDVILMDLEMPRMDGVEATRRI-MAERPC----- 74
                          90       100
                  ....*....|....*....|...
gi 18379305  1001 lewhlPILAMTADV---IHATYE 1020
Cdd:PRK12555   75 -----PILIVTSLTernASRVFE 92
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
923-1036 2.20e-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: 44.67  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALgLLQIPHTFDACFMDIQMPQMDGFEATRQIRMmeketkektnlE 1002
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAV-RRIIDEQPSLVVLDIMLPGMDGLTVCREVRE-----------H 68
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1003 WHLPILAMTADVIHATYEECLKSGMDGYVSKPFE 1036
Cdd:cd19939   69 SHVPILMLTARTEEMDRVLGLEMGADDYLCKPFS 102
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
923-1036 2.60e-05

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 44.68  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMmeketkektnlE 1002
Cdd:cd17622    2 RILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIA-REKPDAVLLDIMLPGIDGLTLCRDLRP-----------K 69
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 18379305 1003 WHLPILAMTA---DVIHATyeeCLKSGMDGYVSKPFE 1036
Cdd:cd17622   70 YQGPILLLTAldsDIDHIL---GLELGADDYVVKPVE 103
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
924-1034 2.91e-05

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: 43.93  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQ-IPHTFDACFMDIQMPQMDGFEATRQIrMMEKETKektnle 1002
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEdEQNEIDLILTEVDLPVSSGFKLLSYI-MRHKICK------ 73
                         90       100       110
                 ....*....|....*....|....*....|..
gi 18379305 1003 wHLPILAMTADVIHATYEECLKSGMDGYVSKP 1034
Cdd:cd17582   74 -NIPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
924-1049 3.17e-05

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: 44.50  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnlew 1003
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLS-DQPPDVVLLDLKLPDMSGMEILKWIQERSLPT-------- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18379305 1004 hlPILAMTAdviHATYE---ECLKSGMDGYVSKPFEEENLYKSVAKSFK 1049
Cdd:cd17572   72 --SVIVITA---HGSVDiavEAMRLGAYDFLEKPFDADRLRVTVRNALK 115
PRK10816 PRK10816
two-component system response regulator PhoP;
923-1038 3.70e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 46.27  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRmmEKETKektnle 1002
Cdd:PRK10816    2 RVLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLN-EHLPDIAIVDLGLPDEDGLSLIRRWR--SNDVS------ 72
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18379305  1003 whLPILAMTADVIHATYEECLKSGMDGYVSKPFEEE 1038
Cdd:PRK10816   73 --LPILVLTARESWQDKVEVLSAGADDYVTKPFHIE 106
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
924-1034 3.85e-05

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


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 43.59  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVAL-GLLQIPHtfDACFMDIQMPQMDGFEATRQIRmmeketkEKTNle 1002
Cdd:cd19936    1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALdGLNARPP--DLAILDIKMPRMDGMELLQRLR-------QKST-- 69
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1003 whLPILAMTA--DVIHATYEecLKSGMDGYVSKP 1034
Cdd:cd19936   70 --LPVIFLTSkdDEIDEVFG--LRMGADDYITKP 99
PRK10336 PRK10336
two-component system response regulator QseB;
924-1035 5.85e-05

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 45.66  E-value: 5.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   924 ILVVDDNIVNRRVAAGaLKKFGAEV---VCAESGQVALglLQIPhtFDACFMDIQMPQMDGFEATRQIRmmEKETKEktn 1000
Cdd:PRK10336    4 LLIEDDMLIGDGIKTG-LSKMGFSVdwfTQGRQGKEAL--YSAP--YDAVILDLTLPGMDGRDILREWR--EKGQRE--- 73
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 18379305  1001 lewhlPILAMTADVIHATYEECLKSGMDGYVSKPF 1035
Cdd:PRK10336   74 -----PVLILTARDALAERVEGLRLGADDYLCKPF 103
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
924-1040 8.51e-05

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: 43.17  E-value: 8.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektnlew 1003
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKL-YDYDIILLDLNLPDMSGYEVLRTLRLAKVKT-------- 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 18379305 1004 hlPILAMT--ADVIHATyeECLKSGMDGYVSKPFEEENL 1040
Cdd:cd17616   72 --PILILSglADIEDKV--KGLGFGADDYMTKPFHKDEL 106
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
923-1036 9.86e-05

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 46.02  E-value: 9.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIrmmeketKEKTNLe 1002
Cdd:PRK10923    5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALA-SKTPDVLLSDIRMPGMDGLALLKQI-------KQRHPM- 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18379305  1003 whLPILAMTA----DVIHATYEEclksGMDGYVSKPFE 1036
Cdd:PRK10923   76 --LPVIIMTAhsdlDAAVSAYQQ----GAFDYLPKPFD 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
923-1038 1.35e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 45.53  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKF-GAEVVC-AESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIrMMEKETkektn 1000
Cdd:PRK00742    5 RVLVVDDSAFMRRLISEILNSDpDIEVVGtAPDGLEAREKIK-KLNPDVITLDVEMPVMDGLDALEKI-MRLRPT----- 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 18379305  1001 lewhlPIL---AMTADVIHATYeECLKSG-MDgYVSKPFEEE 1038
Cdd:PRK00742   78 -----PVVmvsSLTERGAEITL-RALELGaVD-FVTKPFLGI 112
PRK10766 PRK10766
two-component system response regulator TorR;
921-1036 1.38e-04

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 44.26  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   921 GKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMMEketkektn 1000
Cdd:PRK10766    2 SYHILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHV-DLILLDINLPGEDGLMLTRELRSRS-------- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 18379305  1001 lewHLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFE 1036
Cdd:PRK10766   73 ---TVGIILVTGrtdsiDRIVG-----LEMGADDYVTKPLE 105
ompR PRK09468
osmolarity response regulator; Provisional
921-1035 1.44e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 44.58  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   921 GKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQvALGLLQIPHTFDACFMDIQMPQMDGFEATRQIRMMEKETkektn 1000
Cdd:PRK09468    5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAE-QMDRLLTRESFHLMVLDLMLPGEDGLSICRRLRSQNNPT----- 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 18379305  1001 lewhlPILAMTADVIHATYEECLKSGMDGYVSKPF 1035
Cdd:PRK09468   79 -----PIIMLTAKGEEVDRIVGLEIGADDYLPKPF 108
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
924-1034 1.57e-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: 41.97  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLqIPHTFDACFMDIQMPQMDGFEATRQIRmmeketkeKTNLEW 1003
Cdd:cd17602    1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTL-LNSKPDLILIDIDMPDLDGYELCSLLR--------KSSALK 71
                         90       100       110
                 ....*....|....*....|....*....|....
gi 18379305 1004 HLPILAMTADvihATYEECLKSGM---DGYVSKP 1034
Cdd:cd17602   72 DTPIIMLTGK---DGLVDRIRAKMagaSGYLTKP 102
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
923-1040 1.77e-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: 42.23  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVC--AESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRmmekETKEKTN 1000
Cdd:cd19925    2 NVLIVEDDPMVAEIHRAYVEQVPGFTVIgtAGTGEEALKLLKERQP-DLILLDIYLPDGNGLDLLRELR----AAGHDVD 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18379305 1001 lewhlpILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:cd19925   77 ------VIVVTAANDVETVREALRLGVVDYLIKPFTFERL 110
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-721 1.80e-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: 41.60  E-value: 1.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18379305  654 FDISSNVRLMvsIEDTGIGIPLVAQGRVFMPFMQADssTSRNYGGTGIGLSISKCLVELMRGQINFIS 721
Cdd:cd16923   27 FLTDDVVNIM--FKNPSSHPLDFKLEKLFERFYRGD--NSRNTEGAGLGLSIAKAIIELHGGSASAEY 90
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
924-1035 1.98e-04

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


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 41.56  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTFDACFMDIQMP-QMDGFEATRQIRMMEKetkektnle 1002
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPDIDLLVTDVIMPgGMNGSQLAEEARRRRP--------- 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 18379305 1003 wHLPILAMTADVIHATYEECLKSGMDgYVSKPF 1035
Cdd:cd18161   72 -DLKVLLTSGYAENAIEGGDLAPGVD-VLSKPF 102
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
922-1046 2.06e-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: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  922 KKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnl 1001
Cdd:cd17553    1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVT-KERPDLVLLDMKIPGMDGIEILKRMKVIDENIR----- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 18379305 1002 ewhlpILAMTA----DVIhatyEECLKSGMDGYVSKPFEEENLYKSVAK 1046
Cdd:cd17553   75 -----VIIMTAygelDMI----QESKELGALTHFAKPFDIDEIRDAVKK 114
PLN03029 PLN03029
type-a response regulator protein; Provisional
924-1040 2.08e-04

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 43.87  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQI-------PHT------------FDACFMDIQMPQMDGFEa 984
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLheddrsnPDTpsvspnshqeveVNLIITDYCMPGMTGYD- 89
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18379305   985 trqirmMEKETKEKTNLEwHLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENL 1040
Cdd:PLN03029   90 ------LLKKIKESSSLR-NIPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
PRK10643 PRK10643
two-component system response regulator PmrA;
923-1040 2.09e-04

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 43.87  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHtFDACFMDIQMPQMDGFEATRQIRmmeketKEKTNle 1002
Cdd:PRK10643    2 KILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGH-YSLVVLDLGLPDEDGLHLLRRWR------QKKYT-- 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18379305  1003 whLPILAMTA-----DVIHAtyeecLKSGMDGYVSKPFEEENL 1040
Cdd:PRK10643   73 --LPVLILTArdtleDRVAG-----LDVGADDYLVKPFALEEL 108
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
924-1046 2.14e-04

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: 43.55  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfdAC-FMDIQMPQMDGFEATRQIRmmeketkektNLE 1002
Cdd:COG4566    2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRP--GClLLDVRMPGMSGLELQEELA----------ARG 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 18379305 1003 WHLPILAMTAdviHATYEEC---LKSG-MDgYVSKPFEEENLYKSVAK 1046
Cdd:COG4566   70 SPLPVIFLTG---HGDVPMAvraMKAGaVD-FLEKPFDDQALLDAVRR 113
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
924-1034 2.84e-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: 40.89  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNivnrRVAAGALKK----FGAEVVCAESGQVALGLLQIpHTFDACFMDIQMPQMDGFEATRQIRMMEKETkekt 999
Cdd:cd19935    1 ILVVEDE----KKLAEYLKKglteEGYAVDVAYDGEDGLHLALT-NEYDLIILDVMLPGLDGLEVLRRLRAAGKQT---- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 18379305 1000 nlewhlPILAMTA-----DVIHAtyeecLKSGMDGYVSKP 1034
Cdd:cd19935   72 ------PVLMLTArdsveDRVKG-----LDLGADDYLVKP 100
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
452-739 3.08e-04

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 44.19  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   452 QFLATVSHEIRTPMNGILgmlamlLDTELsstqrdYAQTAQVCGKALIALINEVLDraKIE-------AGKlELESVPFD 524
Cdd:PRK10755  139 LFTADVAHELRTPLAGIR------LHLEL------LEKQHHIDVAPLIARLDQMMH--TVEqllqlarAGQ-SFSSGHYQ 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   525 IRSILDDV-LSLFSE-----ESRNKSIELavfVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKG-HIFVKVHLAEQSk 597
Cdd:PRK10755  204 TVKLLEDViLPSQDElsemlEQRQQTLLL---PESAADITVQGDATLLRLLLRNLVENAHRYSPEGsTITIKLSQEDGG- 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   598 desepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrLMVSIEDTGIGIPLVA 677
Cdd:PRK10755  280 ----------------------------------------------------------------AVLAVEDEGPGIDESK 295
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18379305   678 QGRVFMPFMQADSstsrNYGGTGIGLSISKCLVELMRGQINFISRPHIGST---FWFTAVLEKCD 739
Cdd:PRK10755  296 CGELSKAFVRMDS----RYGGIGLGLSIVSRITQLHHGQFFLQNRQERSGTrawVWLPKAQNVAN 356
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
923-1040 3.74e-04

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: 41.27  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAES-GQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMMEKEtkektnl 1001
Cdd:cd17530    2 RVLVLDDDPFQCMMAATILEDLGPGNVDEADdGREALVILLCNAP-DIIICDLKMPDMDGIEFLRHLAESHSN------- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 18379305 1002 ewHLPIL--AMTADVIHATYEECLKSGMD--GYVSKPFEEENL 1040
Cdd:cd17530   74 --AAVILmsGLDGGILESAETLAGANGLNllGTLSKPFSPEEL 114
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
951-1033 3.87e-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: 41.10  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  951 AESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnlewhlpILAMTADVIHATYEECLKSGMDGY 1030
Cdd:cd19930   30 ASNGQEALRLVL-KHSPDVAILDIEMPGRTGLEVAAELREELPDTK----------VLIVTTFGRPGYFRRALAAGVDGY 98

                 ...
gi 18379305 1031 VSK 1033
Cdd:cd19930   99 VLK 101
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
924-1044 7.48e-04

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 42.32  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGL-LQIPHTFDACFMDIQMPQMDGFEATRQIRMMEKETKektnle 1002
Cdd:PRK10651    9 ILLIDDHPMLRTGVKQLISMAPDITVVGEASNGEQGIeLAESLDPDLILLDLNMPGMNGLETLDKLREKSLSGR------ 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18379305  1003 whlpILAMT-----ADVIHAtyeecLKSGMDGYVSKPFEEENLYKSV 1044
Cdd:PRK10651   83 ----IVVFSvsnheEDVVTA-----LKRGADGYLLKDMEPEDLLKAL 120
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
923-1035 8.42e-04

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 42.26  E-value: 8.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKEtkektnle 1002
Cdd:PRK11083    5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLR-QQPPDLVILDVGLPDISGFELCRQLLAFHPA-------- 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 18379305  1003 whLPILAMTadvihATYEEC-----LKSGMDGYVSKPF 1035
Cdd:PRK11083   76 --LPVIFLT-----ARSDEVdrlvgLEIGADDYVAKPF 106
PRK15369 PRK15369
two component system response regulator;
923-1033 8.92e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 41.99  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDN--IVNR-RVAAGALKKFgaEVVcaesGQVALGLlqipHTFDAC--------FMDIQMPQMDGFEATRQIRMm 991
Cdd:PRK15369    5 KILLVDDHelIINGiKNMLAPYPRY--KIV----GQVDNGL----EVYNACrqlepdivILDLGLPGMNGLDVIPQLHQ- 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18379305   992 eketkektnlEW-HLPILAMTADVIHATYEECLKSGMDGYVSK 1033
Cdd:PRK15369   74 ----------RWpAMNILVLTARQEEHMASRTLAAGALGYVLK 106
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
923-1035 1.20e-03

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: 39.67  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQiPHTFDACFMDIQMPQMDGFEATRQIRMMEKetkektnle 1002
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVR-HTPPDLILLDLMLPGTDGLTLCREIRRFSD--------- 70
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 18379305 1003 whLPILAMTADVihatyEEC-----LKSGMDGYVSKPF 1035
Cdd:cd19938   71 --VPIIMVTARV-----EEIdrllgLELGADDYICKPY 101
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
921-1050 1.27e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 41.63  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   921 GKKILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTfDACFMDIQMPQMDGFEATRQIRMmEKETKEktn 1000
Cdd:PRK10161    2 ARRILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWP-DLILLDWMLPGGSGIQFIKHLKR-ESMTRD--- 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18379305  1001 lewhLPILAMTADVIHATYEECLKSGMDGYVSKPFEEENLY---KSVAKSFKP 1050
Cdd:PRK10161   77 ----IPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELVariKAVMRRISP 125
PRTases_typeI cd06223
Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The ...
868-951 1.48e-03

Phosphoribosyl transferase (PRT)-type I domain; Phosphoribosyl transferase (PRT) domain. The type I PRTases are identified by a conserved PRPP binding motif which features two adjacent acidic residues surrounded by one or more hydrophobic residue. PRTases catalyze the displacement of the alpha-1'-pyrophosphate of 5-phosphoribosyl-alpha1-pyrophosphate (PRPP) by a nitrogen-containing nucleophile. The reaction products are an alpha-1 substituted ribose-5'-phosphate and a free pyrophosphate (PP). PRPP, an activated form of ribose-5-phosphate, is a key metabolite connecting nucleotide synthesis and salvage pathways. The type I PRTase family includes a range of diverse phosphoribosyl transferase enzymes and regulatory proteins of the nucleotide synthesis and salvage pathways, including adenine phosphoribosyltransferase EC:2.4.2.7., hypoxanthine-guanine-xanthine phosphoribosyltransferase, hypoxanthine phosphoribosyltransferase EC:2.4.2.8., ribose-phosphate pyrophosphokinase EC:2.7.6.1., amidophosphoribosyltransferase EC:2.4.2.14., orotate phosphoribosyltransferase EC:2.4.2.10., uracil phosphoribosyltransferase EC:2.4.2.9., and xanthine-guanine phosphoribosyltransferase EC:2.4.2.22.


Pssm-ID: 206754 [Multi-domain]  Cd Length: 130  Bit Score: 39.69  E-value: 1.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  868 DRAKSAGFADTVIMKPLRASMI-GACLQQVLE-----LRKTRQQHPEGSS-----PATLKSLLTGKKILVVDDnIVNR-- 934
Cdd:cd06223    7 EEIREDLLEPDVVVGILRGGLPlAAALARALGlplafIRKERKGPGRTPSepyglELPLGGDVKGKRVLLVDD-VIATgg 85
                         90
                 ....*....|....*....
gi 18379305  935 --RVAAGALKKFGAEVVCA 951
Cdd:cd06223   86 tlLAAIELLKEAGAKVVGV 104
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
454-705 1.69e-03

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 42.23  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   454 LATVSHEIRTPMNGILGMLAML------------LDTElssTQRdyaqtaqvcgkaLIALINE--VLDRAKIeagKLELE 519
Cdd:PRK09470  247 LSDISHELRTPLTRLQLATALLrrrqgeskelerIETE---AQR------------LDSMINDllVLSRNQQ---KNHLE 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   520 SVPFDIRSILDDVL--SLFSEESRNKSIElavFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTeKGHIfvKVHLAEQSK 597
Cdd:PRK09470  309 RETFKANSLWSEVLedAKFEAEQMGKSLT---VSAPPGPWPINGNPNALASALENIVRNALRYS-HTKI--EVAFSVDKD 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   598 DesepknalnggvseemivvskqssyntlsgyeaadgrnswdsfkhlvseeqslsefdissnvrLMVSIEDTGIGIPLVA 677
Cdd:PRK09470  383 G---------------------------------------------------------------LTITVDDDGPGVPEEE 399
                         250       260
                  ....*....|....*....|....*...
gi 18379305   678 QGRVFMPFMQADSSTSRNYGGTGIGLSI 705
Cdd:PRK09470  400 REQIFRPFYRVDEARDRESGGTGLGLAI 427
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
661-735 1.88e-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: 39.09  E-value: 1.88e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18379305  661 RLMVSIEDTGIGIPLVAQGRVFMPFMqADSSTSRNYG-GTGIGLSISKCLVELMRGQI--NFISRPHIGSTFWFTAVL 735
Cdd:cd16953   33 MVTISVEDEGPGIPQEKLESIFDRFY-TERPANEAFGqHSGLGLSISRQIIEAHGGISvaENHNQPGQVIGARFTVQL 109
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
924-1041 2.43e-03

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


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 39.24  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  924 ILVVDDNI-VNRRVAAGALKKFGAE--VVCAESGQVALGL---LQIPHTFDACFM-DIQMPQMDGFEATRQIRMMEKETK 996
Cdd:cd17595    3 ILTVDDDPqVLRAVARDLRRQYGKDyrVLRADSGAEALDAlkeLKLRGEAVALFLvDQRMPEMDGVEFLEKAMELFPEAK 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 18379305  997 EKTnlewhLPILAMTADVIHATYEeclkSGMDGYVSKPFE--EENLY 1041
Cdd:cd17595   83 RVL-----LTAYADTDAAIRAIND----VQLDYYLLKPWDppEEKLY 120
PRK11517 PRK11517
DNA-binding response regulator HprR;
923-1035 3.03e-03

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 40.27  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   923 KILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALgLLQIPHTFDACFMDIQMPQMDGFEATRQIRmmekeTKEKTnle 1002
Cdd:PRK11517    2 KILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGL-YLALKDDYALIILDIMLPGMDGWQILQTLR-----TAKQT--- 72
                          90       100       110
                  ....*....|....*....|....*....|...
gi 18379305  1003 whlPILAMTADVIHATYEECLKSGMDGYVSKPF 1035
Cdd:PRK11517   73 ---PVICLTARDSVDDRVRGLDSGANDYLVKPF 102
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
449-599 3.08e-03

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 41.46  E-value: 3.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   449 AKSQFLATVSHEIRTPMNGILGMLAMLLDTELSSTQRDYAQTAQVCGKALIALINEVLDRAKIEAGKLELESVPFDIRSI 528
Cdd:PRK10618  449 ARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDL 528
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18379305   529 LDDVLSLFSEESRNKSIELAVFVSDKVPEIVKGDSGRFRQIIINLVGNSVKFTEKGHIFVKVHLAEQSKDE 599
Cdd:PRK10618  529 IDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVDQDESSPDR 599
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
662-729 4.14e-03

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: 38.77  E-value: 4.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18379305  662 LMVSIEDTGIGIPLVAQGRVFMPFMQADSSTSrnygGTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:cd16954   68 LHLIVDDDGPGVPESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSDSPLGGARF 131
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
659-729 4.16e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 41.05  E-value: 4.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18379305   659 NVRLMVSIEDTGIGIPLVAQGRVFMpfmQADSSTSRNyggTGIGLSISKCLVELMRGQINFISRPHIGSTF 729
Cdd:PRK11086  465 NGWLHCEVSDDGPGIAPDEIDAIFD---KGYSTKGSN---RGVGLYLVKQSVENLGGSIAVESEPGVGTQF 529
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
924-1035 5.87e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 39.40  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305   924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQvaLGLLQI-PHTFDACFMDIQMPQMDGFEATRQIRmmeketkektnlE 1002
Cdd:PRK10529    4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQ--RGLLEAaTRKPDLIILDLGLPDGDGIEFIRDLR------------Q 69
                          90       100       110
                  ....*....|....*....|....*....|....
gi 18379305  1003 WH-LPILAMTADVIHATYEECLKSGMDGYVSKPF 1035
Cdd:PRK10529   70 WSaIPVIVLSARSEESDKIAALDAGADDYLSKPF 103
PRK13557 PRK13557
histidine kinase; Provisional
924-996 6.67e-03

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 40.42  E-value: 6.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18379305   924 ILVVDDNIVNRRVAAGALKKFGAEVVCAESGQVALGLLQIPHTFDACFMDIQMP-QMDGFEATRQIRMMEKETK 996
Cdd:PRK13557  418 ILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPgGMNGVMLAREARRRQPKIK 491
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
654-732 8.25e-03

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: 37.27  E-value: 8.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379305  654 FDISSNVRLmvSIEDTGIGIPLVAQGRVFMPFMQadSSTSRNYG-GTGIGLSISKCLVELMRGQINFISRPHIGSTFWFT 732
Cdd:cd16948   32 ETNEQGVVL--SIKDFGIGIPEEDLPRVFDKGFT--GENGRNFQeSTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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