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Conserved domains on  [gi|951237553|ref|WP_057690214|]
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ATP-binding protein [Acinetobacter baumannii]

Protein Classification

sensor histidine kinase family protein( domain architecture ID 1001650)

sensor histidine kinase family protein, part of a two-component regulatory system, functions as a protein kinase that phosphorylates a target protein in response to various signals; may be a hybrid sensor histidine kinase/response regulator

CATH:  3.30.565.10
EC:  2.7.13.3
PubMed:  10637609|10339418
SCOP:  4001957

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
228-931 5.89e-159

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: 490.13  E-value: 5.89e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 228 GELRLLQRDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNS 307
Cdd:PRK11107 231 GELDMLKNGINAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNG 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 308 IDGFIHLLLRQQnLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIA 387
Cdd:PRK11107 311 VIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLE 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 388 MAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFS 467
Cdd:PRK11107 390 LTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 468 QGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEdnqerAPTDKGSTFWFTAQFAVDEEHEIEHPHFEHLQ---VVSYLA 544
Cdd:PRK11107 470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFH-----SQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAgkrLLYVEP 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 545 HPATASVLRYYL--ENYQVPHIETqsildlfsrLKHLDQKDNTWLIVDHS-------GDTEALLKEIRSRyQGN--LAVY 613
Cdd:PRK11107 545 NSAAAQATLDILseTPLEVTYSPT---------LSQLPEAHYDILLLGLPvtfreplTMLHERLAKAKSM-TDFliLALP 614
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 614 GYQMTLEPNMLTEYRARPLYQPLSRSGLIQLLSDQ----PIFEEEQQDFNGQGLHILAVDDHLPNLIVLEALLGELNVKT 689
Cdd:PRK11107 615 CHEQVLAEQLKQDGADACLSKPLSHTRLLPALLEPchhkQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHV 694
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 690 TKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldgEMQLPIIALTAHALADEKQKLLKVGM 769
Cdd:PRK11107 695 VLCDSGHQAVEQAKQR------PFDLILMDIQMPGMDGIRACELIRQLPH----NQNTPIIAVTAHAMAGERERLLSAGM 764
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 770 NDYVTKPIQMEQIIQILTQWTKNNFTAQNLAKDHHVVAEALDPEILNWQQSLQLAANKEDLAQDLLKMLVDSFPTELEEM 849
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKV 844
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 850 QQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQfisTLRKERRRADdgfIE-EVMRRFDELglviKEVESAAH 928
Cdd:PRK11107 845 EEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ---QLRSGTSVED---LEpELLELLDEM----ENVARAAK 914

                 ...
gi 951237553 929 QIL 931
Cdd:PRK11107 915 KVL 917
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
228-931 5.89e-159

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 490.13  E-value: 5.89e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 228 GELRLLQRDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNS 307
Cdd:PRK11107 231 GELDMLKNGINAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNG 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 308 IDGFIHLLLRQQnLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIA 387
Cdd:PRK11107 311 VIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLE 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 388 MAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFS 467
Cdd:PRK11107 390 LTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 468 QGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEdnqerAPTDKGSTFWFTAQFAVDEEHEIEHPHFEHLQ---VVSYLA 544
Cdd:PRK11107 470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFH-----SQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAgkrLLYVEP 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 545 HPATASVLRYYL--ENYQVPHIETqsildlfsrLKHLDQKDNTWLIVDHS-------GDTEALLKEIRSRyQGN--LAVY 613
Cdd:PRK11107 545 NSAAAQATLDILseTPLEVTYSPT---------LSQLPEAHYDILLLGLPvtfreplTMLHERLAKAKSM-TDFliLALP 614
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 614 GYQMTLEPNMLTEYRARPLYQPLSRSGLIQLLSDQ----PIFEEEQQDFNGQGLHILAVDDHLPNLIVLEALLGELNVKT 689
Cdd:PRK11107 615 CHEQVLAEQLKQDGADACLSKPLSHTRLLPALLEPchhkQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHV 694
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 690 TKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldgEMQLPIIALTAHALADEKQKLLKVGM 769
Cdd:PRK11107 695 VLCDSGHQAVEQAKQR------PFDLILMDIQMPGMDGIRACELIRQLPH----NQNTPIIAVTAHAMAGERERLLSAGM 764
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 770 NDYVTKPIQMEQIIQILTQWTKNNFTAQNLAKDHHVVAEALDPEILNWQQSLQLAANKEDLAQDLLKMLVDSFPTELEEM 849
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKV 844
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 850 QQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQfisTLRKERRRADdgfIE-EVMRRFDELglviKEVESAAH 928
Cdd:PRK11107 845 EEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ---QLRSGTSVED---LEpELLELLDEM----ENVARAAK 914

                 ...
gi 951237553 929 QIL 931
Cdd:PRK11107 915 KVL 917
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
228-902 8.32e-78

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: 273.58  E-value: 8.32e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  228 GELRLLQRDIANVVKRLHFSFL----ELKEHTEQTEE-------DLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLAN 296
Cdd:TIGR02956 391 GRAIEAFRDTAAHNLKLQADERqvaqELQEHKESLEQlvaqrtqELAETNERLNAEVKNHAKARAEAEEANRAKSAFLAT 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  297 ISHELRTPLNSIDGFIHlLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDM 376
Cdd:TIGR02956 471 MSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHL 549
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  377 LSPLAAQKHIAMAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMehddIGQCLLHFSVQDSGIGLSG 456
Cdd:TIGR02956 550 MVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----NDDSSLLFEVEDTGCGIAE 625
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  457 TDRKKLFESFSQGDAsvTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFTAQFAVDEEHEIehphfeh 536
Cdd:TIGR02956 626 EEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESEL-----GVGSCFWFTLPLTRGKPAED------- 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  537 lqvvsylahPATASVLryylenyQVPhietqsildlfsrlkhldqkdntwlivdhsgdteallkeirsryqgnlavygyq 616
Cdd:TIGR02956 692 ---------SATLTVI-------DLP------------------------------------------------------ 701
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  617 mtlepnmlteyrarplyqplsrsgliqllsdqpifeeeqqdfngqGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQ 696
Cdd:TIGR02956 702 ---------------------------------------------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQ 736
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  697 EALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDgemQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:TIGR02956 737 SALECFHQ------HAFDLALLDINLPDGDGVTLLQQLRAIYGAKN---EVKFIAFSAHVFNEDVAQYLAAGFDGFLAKP 807
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  777 IQMEQIIQILTQW---TKNNFTAQNLAK----DHHVVAEALDPE-ILNWQQSLQLAANKEDLAQD-----------LLKM 837
Cdd:TIGR02956 808 VVEEQLTAMIAVIlagGKSNTEAPVLSAspsfDSASVIENAQADdIPESNQASEFLLDEEQLQQDievlgvekvrqLVAL 887
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951237553  838 LVDSFPTELEEMQQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQFISTLRKERRRAD 902
Cdd:TIGR02956 888 FKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSDID 952
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
193-518 1.51e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.90  E-value: 1.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 193 NFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQRDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQ 272
Cdd:COG0642   12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 273 NITYRQARDQAIS-SNQAKSVFLANISHELRTPLNSIDGFIHLLLRQqnLSNEQNLYLQTIRKSSAHLLALINDVLDFSK 351
Cdd:COG0642   92 LLLLLLALLLLLEeANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 352 IDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPqQVIGDALRFKQILTNLISNAIKFTPDG-EIIVR 430
Cdd:COG0642  170 LEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVS 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 431 VRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASvtRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptD 510
Cdd:COG0642  249 VRREGDRV-----RISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEP-----G 316

                 ....*...
gi 951237553 511 KGSTFWFT 518
Cdd:COG0642  317 KGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
407-521 3.14e-50

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: 172.29  E-value: 3.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 407 FKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAI 486
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 487 SKQLVHLMHGQIGFEDNQeraptDKGSTFWFTAQF 521
Cdd:cd16922   81 SKKLVELMGGDISVESEP-----GQGSTFTFTLPL 110
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
293-518 3.87e-33

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 136.04  E-value: 3.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSIDGFIHLL----LRQQNLSNEqnlYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEE 368
Cdd:NF033092 375 FVANVSHELRTPLTTMRSYLEALadgaWKDPELAPR---FLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFNE 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 369 AVFDVMDMLSPLAAQKHIAmafyYADNIPQQVI---GDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllH 444
Cdd:NF033092 452 FFNYIIDRFEMILKNKNIT----FKREFPKRDLwveIDTDKITQVLDNIISNAIKYSPEgGTITFRLLETHNRI-----I 522
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951237553 445 FSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIgFEDNQEraptDKGSTFWFT 518
Cdd:NF033092 523 ISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRI-WAESEE----GKGTTIYFT 591
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
402-518 1.28e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.51  E-value: 1.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553   402 GDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASvTRQFGGT 480
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHV-----EITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 951237553   481 GLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEP-----GGGTTFTIT 107
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
665-786 1.14e-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: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLEStldge 744
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKE------ERPDLILLDINMPGMDGLELLKRIRRRDP----- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 951237553  745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:pfam00072  70 -TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
293-488 9.54e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 106.26  E-value: 9.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSI---DGFIHLllrqqnlsNEQNLYLQTIRksSAHLL--------ALINDVLDFSKIDAGKLELET 361
Cdd:NF040691 274 FVSDVSHELRTPLTTIrmaADVIHD--------SRDDFDPATAR--SAELLhteldrfeSLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 362 APFDLEEAVFDVMDMLSPLAAQKHIAMAFyyadNIPQQ---VIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDI 438
Cdd:NF040691 344 EPVDLRPLVRRVVDALRQLAERAGVELRV----DAPGTpvvAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAV 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 439 GqcllhFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISK 488
Cdd:NF040691 420 A-----VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIAL 464
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
288-501 1.36e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 102.21  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 288 QAKSVFLANISHELRTPLNSIDGFIHLLlrQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLE 367
Cdd:NF012163 238 QMRRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLV 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 368 EAVFDVMDMLSPLAAQKHIAMAFYYADNIpqQVIGDALRFKQILTNLISNAIKFTPDGEiivRVRMEHDDIGQcLLHFSV 447
Cdd:NF012163 316 PLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG---SLHISASQRPK-EVTLTV 389
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 951237553 448 QDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFE 501
Cdd:NF012163 390 ADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAA 443
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
285-504 5.45e-13

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 71.56  E-value: 5.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 285 SSNQAKSVFLANISHELRTPLN--------SIDG--------FIHLLLRQQNLSNeqnlylqtirkssahllaLINDVLD 348
Cdd:NF012226 133 SSVKNAQVWNAAIAHELRTPITilqgrlqgILDGvfepdpalFKSLLNQVEGLSH------------------LVEDLRT 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 349 FSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFyyadNIP-QQVIGDALRFKQILTNLISNAIKFTPDGEI 427
Cdd:NF012226 195 LSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVL----NLTaTPVFCDRRRIEQVLIALIDNAIRYANAGKL 270
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553 428 IVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQ 504
Cdd:NF012226 271 KISSSVIQDD-----WILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQ 342
resp_reg_YycF NF040534
response regulator YycF;
665-783 1.23e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 56.65  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldgE 744
Cdd:NF040534   3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEE-----EVP-DLVLLDIMLPGRDGMEVCREVRK-------K 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:NF040534  70 YDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELI 108
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
228-931 5.89e-159

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 490.13  E-value: 5.89e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 228 GELRLLQRDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNS 307
Cdd:PRK11107 231 GELDMLKNGINAMAMSLSAYHEEMQQNIDQATSDLRETLEQMEIQNVELDLAKKRAQEAARIKSEFLANMSHELRTPLNG 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 308 IDGFIHLLLRQQnLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIA 387
Cdd:PRK11107 311 VIGFTRQTLKTP-LTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLVLENIPFSLRETLDEVVTLLAHSAHEKGLE 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 388 MAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFS 467
Cdd:PRK11107 390 LTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRALSNTKVQLEVQIRDTGIGISERQQSQLFQAFR 469
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 468 QGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEdnqerAPTDKGSTFWFTAQFAVDEEHEIEHPHFEHLQ---VVSYLA 544
Cdd:PRK11107 470 QADASISRRHGGTGLGLVITQKLVNEMGGDISFH-----SQPNRGSTFWFHLPLDLNPNPIIDGLPTDCLAgkrLLYVEP 544
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 545 HPATASVLRYYL--ENYQVPHIETqsildlfsrLKHLDQKDNTWLIVDHS-------GDTEALLKEIRSRyQGN--LAVY 613
Cdd:PRK11107 545 NSAAAQATLDILseTPLEVTYSPT---------LSQLPEAHYDILLLGLPvtfreplTMLHERLAKAKSM-TDFliLALP 614
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 614 GYQMTLEPNMLTEYRARPLYQPLSRSGLIQLLSDQ----PIFEEEQQDFNGQGLHILAVDDHLPNLIVLEALLGELNVKT 689
Cdd:PRK11107 615 CHEQVLAEQLKQDGADACLSKPLSHTRLLPALLEPchhkQPPLLPPTDESRLPLTVMAVDDNPANLKLIGALLEEQVEHV 694
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 690 TKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldgEMQLPIIALTAHALADEKQKLLKVGM 769
Cdd:PRK11107 695 VLCDSGHQAVEQAKQR------PFDLILMDIQMPGMDGIRACELIRQLPH----NQNTPIIAVTAHAMAGERERLLSAGM 764
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 770 NDYVTKPIQMEQIIQILTQWTKNNFTAQNLAKDHHVVAEALDPEILNWQQSLQLAANKEDLAQDLLKMLVDSFPTELEEM 849
Cdd:PRK11107 765 DDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEPVHFPNATLDWQLALRQAAGKPDLARDMLQMLLDFLPEVRNKV 844
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 850 QQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQfisTLRKERRRADdgfIE-EVMRRFDELglviKEVESAAH 928
Cdd:PRK11107 845 EEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQ---QLRSGTSVED---LEpELLELLDEM----ENVARAAK 914

                 ...
gi 951237553 929 QIL 931
Cdd:PRK11107 915 KVL 917
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
228-902 8.32e-78

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: 273.58  E-value: 8.32e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  228 GELRLLQRDIANVVKRLHFSFL----ELKEHTEQTEE-------DLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLAN 296
Cdd:TIGR02956 391 GRAIEAFRDTAAHNLKLQADERqvaqELQEHKESLEQlvaqrtqELAETNERLNAEVKNHAKARAEAEEANRAKSAFLAT 470
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  297 ISHELRTPLNSIDGFIHlLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDM 376
Cdd:TIGR02956 471 MSHEIRTPLNGILGTLE-LLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHL 549
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  377 LSPLAAQKHIAMAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMehddIGQCLLHFSVQDSGIGLSG 456
Cdd:TIGR02956 550 MVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRVSL----NDDSSLLFEVEDTGCGIAE 625
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  457 TDRKKLFESFSQGDAsvTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFTAQFAVDEEHEIehphfeh 536
Cdd:TIGR02956 626 EEQATLFDAFTQADG--RRRSGGTGLGLAISQRLVEAMDGELGVESEL-----GVGSCFWFTLPLTRGKPAED------- 691
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  537 lqvvsylahPATASVLryylenyQVPhietqsildlfsrlkhldqkdntwlivdhsgdteallkeirsryqgnlavygyq 616
Cdd:TIGR02956 692 ---------SATLTVI-------DLP------------------------------------------------------ 701
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  617 mtlepnmlteyrarplyqplsrsgliqllsdqpifeeeqqdfngqGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQ 696
Cdd:TIGR02956 702 ---------------------------------------------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQ 736
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  697 EALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDgemQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:TIGR02956 737 SALECFHQ------HAFDLALLDINLPDGDGVTLLQQLRAIYGAKN---EVKFIAFSAHVFNEDVAQYLAAGFDGFLAKP 807
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  777 IQMEQIIQILTQW---TKNNFTAQNLAK----DHHVVAEALDPE-ILNWQQSLQLAANKEDLAQD-----------LLKM 837
Cdd:TIGR02956 808 VVEEQLTAMIAVIlagGKSNTEAPVLSAspsfDSASVIENAQADdIPESNQASEFLLDEEQLQQDievlgvekvrqLVAL 887
                         650       660       670       680       690       700
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951237553  838 LVDSFPTELEEMQQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQFISTLRKERRRAD 902
Cdd:TIGR02956 888 FKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLCQQLEKQGKTGALELSDID 952
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
193-518 1.51e-74

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 247.90  E-value: 1.51e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 193 NFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQRDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQ 272
Cdd:COG0642   12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 273 NITYRQARDQAIS-SNQAKSVFLANISHELRTPLNSIDGFIHLLLRQqnLSNEQNLYLQTIRKSSAHLLALINDVLDFSK 351
Cdd:COG0642   92 LLLLLLALLLLLEeANEAKSRFLANVSHELRTPLTAIRGYLELLLEE--LDEEQREYLETILRSADRLLRLINDLLDLSR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 352 IDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPqQVIGDALRFKQILTNLISNAIKFTPDG-EIIVR 430
Cdd:COG0642  170 LEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGIELELDLPDDLP-TVRGDPDRLRQVLLNLLSNAIKYTPEGgTVTVS 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 431 VRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASvtRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptD 510
Cdd:COG0642  249 VRREGDRV-----RISVEDTGPGIPPEDLERIFEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEP-----G 316

                 ....*...
gi 951237553 511 KGSTFWFT 518
Cdd:COG0642  317 KGTTFTVT 324
PRK15347 PRK15347
two component system sensor kinase;
266-893 9.00e-71

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 252.64  E-value: 9.00e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 266 LDTLEVQnitYRQ--------------ARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLLLRQQnLSNEQNLYLQT 331
Cdd:PRK15347 363 LDTLNEQ---YDTlenkvaertqalaeAKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTP-LTAEQMDLADT 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 332 IRKSSAHLLALINDVLDFSKIDAGKLEL---ETAPFDLEEavfDVMDMLSPLAAQKHIAMAFYYADNIPQQVIGDALRFK 408
Cdd:PRK15347 439 ARQCTLSLLAIINNLLDFSRIESGQMTLsleETALLPLLD---QAMLTIQGPAQSKSLTLRTFVGAHVPLYLHLDSLRLR 515
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNAIKFTPDGEIIVRVRMEHDdigqcLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVtrqfGGTGLGLAISK 488
Cdd:PRK15347 516 QILVNLLGNAVKFTETGGIRLRVKRHEQ-----QLCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIAS 586
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 489 QLVHLMHGQIGFEdnqerAPTDKGSTFWFTAQFavdeeHEIEHPHFEHLQVVSYLA-HPATASVLRYYLENYQVPHIETQ 567
Cdd:PRK15347 587 SLAKMMGGELTLF-----STPGVGSCFSLVLPL-----NEYAPPEPLKGELSAPLAlHRQLSAWGITCQPGHQNPALLDP 656
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 568 SILDLFSRLKhldqkdntwlivdhsgdteALLKEIRSryqgnlavygyqmtlepNMLTEYRARPLYQPLSrsgliqllsd 647
Cdd:PRK15347 657 ELAYLPGRLY-------------------DLLQQIIQ-----------------GAPNEPVINLPLQPWQ---------- 690
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 648 qpifeeeqqdfngqgLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIdqklkpFDLVFMDIQMPVMSG 727
Cdd:PRK15347 691 ---------------LQILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHR------FDLVLMDIRMPGLDG 749
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 728 IDTTRAIRSLESTLDGEmqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILtqwtknNFTAQ-NLAKDHHVV 806
Cdd:PRK15347 750 LETTQLWRDDPNNLDPD--CMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL------ELAAEyQLLRGIELS 821
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 807 --AEALDPEIlnwqqSLQLAANKEDLAQDLLKMlvdsfpteLEEMQQLIELEDfpQLEHVLHRLYGATRYVGTPKLQQVT 884
Cdd:PRK15347 822 pqDSSCSPLL-----DTDDMALNSKLYQSLLLL--------LAQIEQAVENQE--VLSQLLHTLKGCAGQAGLTELQCAV 886

                 ....*....
gi 951237553 885 GDFEQFIST 893
Cdd:PRK15347 887 IDLENALET 895
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
277-518 1.22e-70

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 234.03  E-value: 1.22e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 277 RQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLLLRQQNLSNE-QNLYLQTIRKSSAHLLALINDVLDFSKIDAG 355
Cdd:COG2205    3 EEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEDLSPEeRRELLEIIRESAERLLRLIEDLLDLSRLESG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 356 KLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPqQVIGDALRFKQILTNLISNAIKFTPDG-EIIVRVRME 434
Cdd:COG2205   83 KLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELP-LVYADPELLEQVLANLLDNAIKYSPPGgTITISARRE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 435 HDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDAsvTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGST 514
Cdd:COG2205  162 GDGV-----RISVSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEP-----GGGTT 229

                 ....
gi 951237553 515 FWFT 518
Cdd:COG2205  230 FTVT 233
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
155-518 2.16e-70

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 238.68  E-value: 2.16e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 155 VWLLIEMDNQPLELARYRILIALVITGLMTLLLLLLCLNFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQ 234
Cdd:COG5002   30 LLLLLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 235 RDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHL 314
Cdd:COG5002  110 LLILLAALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLEL 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 315 LLRQQNLSNEQNL-YLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYA 393
Cdd:COG5002  190 LLDGAADDPEERReYLEIILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKGIELELDLP 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 394 DNIPQqVIGDALRFKQILTNLISNAIKFTPDG-EIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDAS 472
Cdd:COG5002  270 EDPLL-VLGDPDRLEQVLTNLLDNAIKYTPEGgTITVSLREEDDQV-----RISVRDTGIGIPEEDLPRIFERFYRVDKS 343
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 951237553 473 VTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:COG5002  344 RSRETGGTGLGLAIVKHIVEAHGGRIWVESEP-----GKGTTFTIT 384
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
278-789 6.11e-64

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 232.94  E-value: 6.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 278 QARDQAissNQAKSVFLANISHELRTPLNSIDGFIHLLlRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKL 357
Cdd:PRK10841 438 QAAEQA---SQSKSMFLATVSHELRTPLYGIIGNLDLL-QTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQL 513
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 358 ELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDd 437
Cdd:PRK10841 514 KIEPREFSPREVINHITANYLPLVVKKRLGLYCFIEPDVPVALNGDPMRLQQVISNLLSNAIKFTDTGCIVLHVRVDGD- 592
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 438 igqcLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTF-- 515
Cdd:PRK10841 593 ----YLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEP-----GMGSQFti 663
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 516 ---WFTAQFAVDEEHEIEHPHFEHLQVV-SYLAHPATASVLRYYLE--NYQVPHIETQSIL--DlfsrlkHLDQKD-NTW 586
Cdd:PRK10841 664 ripLYGAQYPQKKGVEGLQGKRCWLAVRnASLEQFLETLLQRSGIQvqRYEGQEPTPEDVLitD------DPVQKKwQGR 737
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 587 LIVDHSGDTEALLKEIRSryqgnlavyGYQM--TLEPNMLTEYRARpLYQP--LSRSGLIQLLSDQPIFEEEQQdfngqg 662
Cdd:PRK10841 738 AVITFCRRHIGIPLEIAP---------GEWVhsTATPHELPALLAR-IYRIelESDDSANALPSTDKAVSDNDD------ 801
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTld 742
Cdd:PRK10841 802 MMILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSK------NHIDIVLTDVNMPNMDGYRLTQRLRQLGLT-- 873
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 951237553 743 gemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQW 789
Cdd:PRK10841 874 ----LPVIGVTANALAEEKQRCLEAGMDSCLSKPVTLDVLKQTLTVY 916
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
273-883 4.30e-56

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 207.87  E-value: 4.30e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 273 NITYR-QARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLLLRQQnLSNEQNLYLQTIRKSSAHLLALINDVLDFSK 351
Cdd:PRK11091 265 DITERkRYQDALEKASRDKTTFISTISHELRTPLNGIVGLSRILLDTE-LTAEQRKYLKTIHVSAITLGNIFNDIIDMDK 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 352 IDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRV 431
Cdd:PRK11091 344 MERRKLQLDNQPIDFTDFLADLENLSGLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV 423
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 432 RMEHDDIgqclLHFSVQDSGIGLSGTDRKKLFESFSQ-GDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptD 510
Cdd:PRK11091 424 RYEEGDM----LTFEVEDSGIGIPEDELDKIFAMYYQvKDSHGGKPATGTGIGLAVSKRLAQAMGGDITVTSEE-----G 494
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 511 KGSTFWFTAQF-AVDEEHEIehphfehlqvvsylahpatasvlryylenyqvphietqsildlfsrlkhldqkdntwliv 589
Cdd:PRK11091 495 KGSCFTLTIHApAVAEEVED------------------------------------------------------------ 514
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 590 dhsgdteallkeirsryqgnlavygyqmtlepnmlteyrarplyqplsrsgliqllsdqpifEEEQQDFNGQGLHILAVD 669
Cdd:PRK11091 515 --------------------------------------------------------------AFDEDDMPLPALNILLVE 532
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 670 DHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSlestLDGEMQL-P 748
Cdd:PRK11091 533 DIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDP------DEYDLVLLDIQLPDMTGLDIARELRE----RYPREDLpP 602
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 749 IIALTAHALADeKQKLLKVGMNDYVTKPIQMEQIIQILTQWTknnftaqnlakdHHVVAEALDPeilnwQQSLQLAANKE 828
Cdd:PRK11091 603 LVALTANVLKD-KKEYLDAGMDDVLSKPLSVPALTAMIKKFW------------DTQDDEESTV-----TTEESSKANEA 664
                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553 829 DLAQDLLKMLVDSFPTEL--------EEM--QQLIELE------DFPQLEHVLHRLYGATRYVGTPKLQQV 883
Cdd:PRK11091 665 LLDIPMLEQYVELVGPKLitdslavfEKMmpGYLSVLDsnltarDQKGIVEEAHKIKGAAGSVGLRHLQQL 735
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
407-521 3.14e-50

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: 172.29  E-value: 3.14e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 407 FKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAI 486
Cdd:cd16922    1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 487 SKQLVHLMHGQIGFEDNQeraptDKGSTFWFTAQF 521
Cdd:cd16922   81 SKKLVELMGGDISVESEP-----GQGSTFTFTLPL 110
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
156-518 4.98e-47

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 176.13  E-value: 4.98e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 156 WLLIEMDNQPLELARYRILIALVITGLMTLLLLLLCLNFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQR 235
Cdd:COG4251  148 ALLLLLLLLLLLLLLLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGL 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 236 DIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLL 315
Cdd:COG4251  228 LLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLL 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 316 LRQ--QNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIdaGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAfyyA 393
Cdd:COG4251  308 EEDygDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV--GRQELEFEPVDLNELLEEVLEDLEPRIEERGAEIE---V 382
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 394 DNIPqQVIGDALRFKQILTNLISNAIKFTPDGEI-IVRVRMEHDDiGQCllHFSVQDSGIGLSGTDRKKLFESFSQGDAS 472
Cdd:COG4251  383 GPLP-TVRGDPTLLRQVFQNLISNAIKYSRPGEPpRIEIGAEREG-GEW--VFSVRDNGIGIDPEYAEKIFEIFQRLHSR 458
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 951237553 473 vtRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:COG4251  459 --DEYEGTGIGLAIVKKIVERHGGRIWVESEP-----GEGATFYFT 497
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
665-786 1.52e-40

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: 144.92  E-value: 1.52e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd17546    1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKE------EPFDLVLMDLQMPVMDGLEATRRIRELEGGGR-- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17546   73 -RTPIIALTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
260-888 2.18e-40

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 161.83  E-value: 2.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  260 EDLRRTLDTLEVQNITyrqaRDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLLlRQQNLSNEQNLYLQTIRKSSAH- 338
Cdd:PRK09959  686 QDITETRDLIHALEVE----RNKAINATVAKSQFLATMSHEIRTPISSIMGFLELL-SGSGLSKEQRVEAISLAYATGQs 760
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  339 LLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFyyADNIPQQ--VIGDALRFKQILTNLIS 416
Cdd:PRK09959  761 LLGLIGEILDVDKIESGNYQLQPQWVDIPTLVQNTCHSFGAIAASKSIALSC--SSTFPDHylVKIDPQAFKQVLSNLLS 838
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  417 NAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFSQgdASVTRQFGGTGLGLAISKQLVHLMHG 496
Cdd:PRK09959  839 NALKFTTEGAVKITTSLGHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQ--TSAGRQQTGSGLGLMICKELIKNMQG 916
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  497 QIGFEdnqeraptdkgstfwftaqfavdeeheiehphfehlqvvsylAHPATASVlryylenyqvphietqsildlfsrl 576
Cdd:PRK09959  917 DLSLE------------------------------------------SHPGIGTT------------------------- 929
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  577 khldqkdntwlivdhsgdteallkeirsryqgnlavygYQMTLEPNMLTEYRArplyqplsrsglIQLLSDQPIFEEEQq 656
Cdd:PRK09959  930 --------------------------------------FTITIPVEISQQVAT------------VEAKAEQPITLPEK- 958
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  657 dfngqgLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQeridqkLKPFDLVFMDIQMPVMSGIDTTRAIRS 736
Cdd:PRK09959  959 ------LSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVS------MQHYDLLITDVNMPNMDGFELTRKLRE 1026
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  737 LESTldgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQWTKnnfTAQNLAKDHHVVAEALDPEiln 816
Cdd:PRK09959 1027 QNSS------LPIWGLTANAQANEREKGLSCGMNLCLFKPLTLDVLKTHLSQLHQ---VAHIAPQYRHLDIEALKNN--- 1094
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951237553  817 wqqslqlAANKEDLAQDLLKMLVDSFPTELEEMQQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFE 888
Cdd:PRK09959 1095 -------TANDLQLMQEILMTFQHETHKDLPAAFHALEAGDNRTFHQCIHRIHGAANILNLQKLINISHQLE 1159
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
274-530 2.64e-39

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: 152.82  E-value: 2.64e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 274 ITYRQARDQAISSNQAKSV---FLANISHELRTPLNSIDGFIHLLlrQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFS 350
Cdd:COG5809  251 ITERKKLEELLRKSEKLSVvgeLAAGIAHEIRNPLTSLKGFIQLL--KDTIDEEQKTYLDIMLSELDRIESIISEFLVLA 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 351 KIDAGKLEletaPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPQqVIGDALRFKQILTNLISNAIKFTPD-GEIIV 429
Cdd:COG5809  329 KPQAIKYE----PKDLNTLIEEVIPLLQPQALLKNVQIELELEDDIPD-ILGDENQLKQVFINLLKNAIEAMPEgGNITI 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 430 RVRMEHDDIgqclLHFSVQDSGIGLSGTDRKKLFESFSqgdasvTRQFGGTGLGLAISKQLVHLMHGQIGFEdnqerAPT 509
Cdd:COG5809  404 ETKAEDDDK----VVISVTDEGCGIPEERLKKLGEPFY------TTKEKGTGLGLMVSYKIIEEHGGKITVE-----SEV 468
                        250       260
                 ....*....|....*....|.
gi 951237553 510 DKGSTFWFTAQFAVDEEHEIE 530
Cdd:COG5809  469 GKGTTFSITLPIKLSEQVSMN 489
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
251-498 4.39e-39

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 156.99  E-value: 4.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 251 LKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLLLRQQnLSNEQNLYLQ 330
Cdd:PRK11466 405 LNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNP-ALNAQRDDLR 483
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 331 TIRKSSAHLLALINDVLDFSKIDAG--KLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPQQVIGDALRFK 408
Cdd:PRK11466 484 AITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIR 563
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNAIKFTPDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFESFSQgdasVTRQFGGTGLGLAISK 488
Cdd:PRK11466 564 QVITNLLSNALRFTDEGSIVLRSRTDGEQ-----WLVEVEDSGCGIDPAKLAEIFQPFVQ----VSGKRGGTGLGLTISS 634
                        250
                 ....*....|
gi 951237553 489 QLVHLMHGQI 498
Cdd:PRK11466 635 RLAQAMGGEL 644
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
233-518 4.82e-39

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: 148.13  E-value: 4.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  233 LQRDIANVVKRLHFS-FLELKeHTEQTEEDLRRTLD--TLEVQNITYR------QARD--QAISSNQAKSVFLANISHEL 301
Cdd:TIGR02966  47 LGQRITNLIRHPEFVeYLAAG-RFSEPLELPSPINSerVLEIRIAPYGeeqkllVARDvtRLRRLEQMRRDFVANVSHEL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  302 RTPLNSIDGFIHLLLRQQNLSNE-QNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPL 380
Cdd:TIGR02966 126 RTPLTVLRGYLETLADGPDEDPEeWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLDHLRDEAEAL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  381 AAQKHIAMAFYYADNIPqqVIGDALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDIGqclLHFSVQDSGIGLSGTDRK 460
Cdd:TIGR02966 206 SQGKNHQITFEIDGGVD--VLGDEDELRSAFSNLVSNAIKYTPEGGTI-TVRWRRDGGG---AEFSVTDTGIGIAPEHLP 279
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553  461 KLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQEraptdKGSTFWFT 518
Cdd:TIGR02966 280 RLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELG-----KGSTFSFI 332
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
155-518 2.67e-37

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 144.17  E-value: 2.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 155 VWLLIEMDNQPLELARYRILIALVITGLMTLLLLLLCLNFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQ 234
Cdd:COG4191   12 LALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 235 RDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLevqnityRQARDQAISSNQAKSV--FLANISHELRTPLNSIDGFI 312
Cdd:COG4191   92 ALLLLLLAALDAEENAELEELERDITELERAEEEL-------RELQEQLVQSEKLAALgeLAAGIAHEINNPLAAILGNA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 313 HLLLR--QQNLSNEQNL-YLQTIRKSSAHLLALINDVLDFSKIDagklELETAPFDLEEAVFDVMDMLSPLAAQKHIAMA 389
Cdd:COG4191  165 ELLRRrlEDEPDPEELReALERILEGAERAAEIVRSLRAFSRRD----EEEREPVDLNELIDEALELLRPRLKARGIEVE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 390 FYYADNIPQqVIGDALRFKQILTNLISNAI---KFTPDGEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESF 466
Cdd:COG4191  241 LDLPPDLPP-VLGDPGQLEQVLLNLLINAIdamEEGEGGRITISTRREGDYV-----VISVRDNGPGIPPEVLERIFEPF 314
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 951237553 467 sqgdasVT--RQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:COG4191  315 ------FTtkPVGKGTGLGLSISYGIVEKHGGRIEVESEP-----GGGTTFTIT 357
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
659-789 3.75e-37

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


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 135.75  E-value: 3.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 659 NGQGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLE 738
Cdd:COG0784    2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAG------PPDLILLDINMPGMDGLELLRRIRALP 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 951237553 739 STLDgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQW 789
Cdd:COG0784   76 RLPD----IPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRL 122
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
297-518 2.27e-34

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: 137.02  E-value: 2.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 297 ISHELRTPLNSIDGFIHLLLR--QQNLSNEQ---NLYLQTIRKSSAHLLALINDVLDFSKIDAGKLEletaPFDLEEAVF 371
Cdd:COG5000  208 IAHEIKNPLTPIQLSAERLRRklADKLEEDRedlERALDTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLR 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 372 DVMDMLSPLAAQKHIAMAFYYADNIPQqVIGDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllHFSVQDS 450
Cdd:COG5000  284 EVLALYEPALKEKDIRLELDLDPDLPE-VLADRDQLEQVLINLLKNAIEAIEEgGEIEVSTRREDGRV-----RIEVSDN 357
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553 451 GIGLSGTDRKKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:COG5000  358 GPGIPEEVLERIFEPF------FTTKPKGTGLGLAIVKKIVEEHGGTIELESRP-----GGGTTFTIR 414
HK_WalK NF033092
cell wall metabolism sensor histidine kinase WalK; This model describes WalK as found in ...
293-518 3.87e-33

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


Pssm-ID: 467964 [Multi-domain]  Cd Length: 594  Bit Score: 136.04  E-value: 3.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSIDGFIHLL----LRQQNLSNEqnlYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEE 368
Cdd:NF033092 375 FVANVSHELRTPLTTMRSYLEALadgaWKDPELAPR---FLGVTQNETERMIRLVNDLLQLSRMDSKDYKLNKEWVNFNE 451
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 369 AVFDVMDMLSPLAAQKHIAmafyYADNIPQQVI---GDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllH 444
Cdd:NF033092 452 FFNYIIDRFEMILKNKNIT----FKREFPKRDLwveIDTDKITQVLDNIISNAIKYSPEgGTITFRLLETHNRI-----I 522
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951237553 445 FSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIgFEDNQEraptDKGSTFWFT 518
Cdd:NF033092 523 ISISDQGLGIPKKDLDKIFDRFYRVDKARSRKMGGTGLGLAIAKEVVEAHGGRI-WAESEE----GKGTTIYFT 591
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
269-501 3.14e-32

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 129.20  E-value: 3.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 269 LEVQNITYR-QARDQAISSNQAKSV--FLANISHELRTPLNSIDGFIHLLlrQQNLSNEQNL-YLQTIRKSSAHLLALIN 344
Cdd:COG3852  111 LVLRDITERkRLERELRRAEKLAAVgeLAAGLAHEIRNPLTGIRGAAQLL--ERELPDDELReYTQLIIEEADRLNNLVD 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 345 DVLDFSKIDAGKLEletaPFDLEEAVFDVMDMLSPLAAqKHIAMAFYYADNIPQqVIGDALRFKQILTNLISNAIKFTPD 424
Cdd:COG3852  189 RLLSFSRPRPPERE----PVNLHEVLERVLELLRAEAP-KNIRIVRDYDPSLPE-VLGDPDQLIQVLLNLVRNAAEAMPE 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 425 -GEIIVRVRMEHDDIGQCLLH-----FSVQDSGIGLSGTDRKKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:COG3852  263 gGTITIRTRVERQVTLGGLRPrlyvrIEVIDNGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGTI 336

                 ...
gi 951237553 499 GFE 501
Cdd:COG3852  337 EVE 339
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
663-784 1.10e-31

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: 121.94  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLESTLD 742
Cdd:COG3706    2 ARILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEH------RPDLILLDLEMPDMDGLELCRRLRADPRTAD 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 951237553 743 gemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQ 784
Cdd:COG3706   76 ----IPIIFLTALDDEEDRARALEAGADDYLTKPFDPEELLA 113
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
402-518 1.28e-29

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 113.51  E-value: 1.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553   402 GDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASvTRQFGGT 480
Cdd:smart00387   1 GDPDRLRQVLSNLLDNAIKYTPEgGRITVTLERDGDHV-----EITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 951237553   481 GLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:smart00387  75 GLGLSIVKKLVELHGGEISVESEP-----GGGTTFTIT 107
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
659-786 1.96e-27

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


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 111.41  E-value: 1.96e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 659 NGQGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLE 738
Cdd:COG3437    3 TGQAPTVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEA------PPDLILLDVRMPGMDGFELLRLLRADP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 951237553 739 STLDgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:COG3437   77 STRD----IPVIFLTALADPEDRERALEAGADDYLTKPFDPEELLARV 120
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
665-786 1.14e-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: 1.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLEStldge 744
Cdd:pfam00072   1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKE------ERPDLILLDINMPGMDGLELLKRIRRRDP----- 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 951237553  745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:pfam00072  70 -TTPVIILTAHGDEDDAVEALEAGADDFLSKPFDPDELLAAI 110
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
402-518 3.59e-26

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 103.60  E-value: 3.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  402 GDALRFKQILTNLISNAIKFTP-DGEIIVRVRMEHDdigqclLHFSVQDSGIGLSGTDRKKLFESFSQGDasvTRQFGGT 480
Cdd:pfam02518   1 GDELRLRQVLSNLLDNALKHAAkAGEITVTLSEGGE------LTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 951237553  481 GLGLAISKQLVHLMHGQIGFEDNQERaptdkGSTFWFT 518
Cdd:pfam02518  72 GLGLSIVRKLVELLGGTITVESEPGG-----GTTVTLT 104
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
407-518 1.50e-25

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


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 101.53  E-value: 1.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 407 FKQILTNLISNAIKFTP-DGEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRqfGGTGLGLA 485
Cdd:cd00075    1 LEQVLSNLLDNALKYSPpGGTIEISLRQEGDGV-----VLEVEDNGPGIPEEDLERIFERFYRGDKSREG--GGTGLGLA 73
                         90       100       110
                 ....*....|....*....|....*....|...
gi 951237553 486 ISKQLVHLMHGQIGFEDNQEraptdKGSTFWFT 518
Cdd:cd00075   74 IVRRIVEAHGGRITVESEPG-----GGTTFTVT 101
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
291-518 5.15e-25

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: 109.40  E-value: 5.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  291 SVFLANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAV 370
Cdd:TIGR01386 242 SQFSADLAHELRTPLTNLLGQTQVALSQPRTGEEYREVLESNLEELERLSRMVSDMLFLARADNGQLALERVRLDLAAEL 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  371 FDVMDMLSPLAAQKHIAMAFyyadNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIvRVRMEhDDIGQCLLhfSVQDS 450
Cdd:TIGR01386 322 AKVAEYFEPLAEERGVRIRV----EGEGLVRGDPQMFRRAISNLLSNALRHTPDGGTI-TVRIE-RRSDEVRV--SVSNP 393
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553  451 GIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQERaptdkgSTFWFT 518
Cdd:TIGR01386 394 GPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK------TRFILR 455
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
293-518 4.91e-24

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 106.25  E-value: 4.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIdagklelETAP-FDLEEAVf 371
Cdd:PRK11006 207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALREKALHTMREQTQRMEGLVKQLLTLSKI-------EAAPtIDLNEKV- 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 372 DVMDMLS-------PLAAQKHiAMAFYYADNIpqQVIGDALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDIGQCllh 444
Cdd:PRK11006 279 DVPMMLRvlereaqTLSQGKH-TITFEVDNSL--KVFGNEDQLRSAISNLVYNAVNHTPEGTHI-TVRWQRVPQGAE--- 351
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951237553 445 FSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQeraptDKGSTFWFT 518
Cdd:PRK11006 352 FSVEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEV-----GKGTRFSFV 420
PRK10490 PRK10490
sensor protein KdpD; Provisional
231-528 7.73e-24

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 108.20  E-value: 7.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 231 RLLQ---RDIANVVKRLHFSflelkehteQTEEdlrrtldtlevqnityrQARDQAiSSNQAKSVFLANISHELRTPLNS 307
Cdd:PRK10490 629 RLLEtftLLIANALERLTLT---------ASEE-----------------QARLAS-EREQLRNALLAALSHDLRTPLTV 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 308 IDGFIHLLLrqQNLSNEQNLYLQTIRKSSAHLLA---LINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQK 384
Cdd:PRK10490 682 LFGQAEILT--LDLASEGSPHARQASEIRQQVLNttrLVNNLLDMARIQSGGFNLRKEWLTLEEVVGSALQMLEPGLSGH 759
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 385 HIAMafyyadNIPQQVI---GDALRFKQILTNLISNAIKFT-PDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRK 460
Cdd:PRK10490 760 PINL------SLPEPLTlihVDGPLFERVLINLLENAVKYAgAQAEIGIDAHVEGER-----LQLDVWDNGPGIPPGQEQ 828
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951237553 461 KLFESFSQGDASVTrqFGGTGLGLAISKQLVHLMHGQIGFEDNQEraptdKGSTFWFTAQF----AVDEEHE 528
Cdd:PRK10490 829 LIFDKFARGNKESA--IPGVGLGLAICRAIVEVHGGTIWAENRPE-----GGACFRVTLPLetppELEEFHE 893
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
293-488 9.54e-24

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 106.26  E-value: 9.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSI---DGFIHLllrqqnlsNEQNLYLQTIRksSAHLL--------ALINDVLDFSKIDAGKLELET 361
Cdd:NF040691 274 FVSDVSHELRTPLTTIrmaADVIHD--------SRDDFDPATAR--SAELLhteldrfeSLLSDLLEISRFDAGAAELDV 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 362 APFDLEEAVFDVMDMLSPLAAQKHIAMAFyyadNIPQQ---VIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDI 438
Cdd:NF040691 344 EPVDLRPLVRRVVDALRQLAERAGVELRV----DAPGTpvvAEVDPRRVERVLRNLVVNAIEHGEGKPVVVTVAQDDTAV 419
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 439 GqcllhFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISK 488
Cdd:NF040691 420 A-----VTVRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIAL 464
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
665-785 9.78e-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: 96.84  E-value: 9.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd17548    2 ILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKE-----KP-DLILMDIQLPGMDGLEATRLLKEDPATRD-- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 951237553 745 mqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQI 785
Cdd:cd17548   74 --IPVIALTAYAMKGDREKILEAGCDGYISKPIDTREFLET 112
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
403-502 1.24e-23

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: 96.41  E-value: 1.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDIGQCLLhfSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGL 482
Cdd:cd16925    1 DAEKYERVVLNLLSNAFKFTPDGGRI-RCILEKFRLNRFLL--TVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                         90       100
                 ....*....|....*....|
gi 951237553 483 GLAISKQLVHLMHGQIGFED 502
Cdd:cd16925   78 GLSIVKEFVELHGGTVTVSD 97
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
663-783 2.14e-23

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: 98.87  E-value: 2.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStld 742
Cdd:COG0745    2 PRILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEE------RPDLILLDLMLPGMDGLEVCRRLRARPS--- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 951237553 743 gemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:COG0745   73 ---DIPIIMLTARDDEEDRVRGLEAGADDYLTKPFDPEELL 110
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
295-501 3.56e-23

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


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 103.02  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 295 ANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLEletaPFDLEEAVFDVM 374
Cdd:COG5806  206 ASIAHEVRNPLTVVRGFIQLLQEPELSDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKLE----KIDVSEELEHVI 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 375 DMLSPLAAQKHIAMAFYYADNIpqQVIGDALRFKQILTNLISNAIKFTPDG---EIIVRVRMEHddigqclLHFSVQDSG 451
Cdd:COG5806  282 DVLSPYANMNNVEIQTELEPGL--YIEGDRQKLQQCLINIIKNGIEAMPNGgtlTIDVSIDKNK-------VIISIKDTG 352
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 452 IGLSGTDRKKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQIGFE 501
Cdd:COG5806  353 VGMTKEQLERLGEPY------FSTKEKGTGLGTMVSYRIIEAMNGTIRVE 396
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
665-777 3.66e-23

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: 94.89  E-value: 3.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd19920    1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAE------PPDLILLDVMMPGMDGFEVCRRLKADPATRH-- 72
                         90       100       110
                 ....*....|....*....|....*....|...
gi 951237553 745 mqLPIIALTAHALADEKQKLLKVGMNDYVTKPI 777
Cdd:cd19920   73 --IPVIFLTALTDTEDKVKGFELGAVDYITKPF 103
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
288-501 1.36e-22

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 102.21  E-value: 1.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 288 QAKSVFLANISHELRTPLNSIDGFIHLLlrQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLE 367
Cdd:NF012163 238 QMRRDFMADISHELRTPLAVLRAELEAI--QDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQKASVDLV 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 368 EAVFDVMDMLSPLAAQKHIAMAFYYADNIpqQVIGDALRFKQILTNLISNAIKFTPDGEiivRVRMEHDDIGQcLLHFSV 447
Cdd:NF012163 316 PLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGG---SLHISASQRPK-EVTLTV 389
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 951237553 448 QDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFE 501
Cdd:NF012163 390 ADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTLHAA 443
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
664-777 9.04e-22

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: 91.02  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSLESTldg 743
Cdd:cd17538    1 KILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEE-----LP-DLILLDVMMPGMDGFEVCRRLKEDPET--- 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 951237553 744 eMQLPIIALTahALADEKQKL--LKVGMNDYVTKPI 777
Cdd:cd17538   72 -RHIPVIMIT--ALDDREDRIrgLEAGADDFLSKPI 104
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
290-503 1.11e-21

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 99.46  E-value: 1.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 290 KSVFLANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEA 369
Cdd:PRK09835 262 QSNFSADIAHEIRTPITNLITQTEIALSQSRSQKELEDVLYSNLEELTRMAKMVSDMLFLAQADNNQLIPEKKMLDLADE 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 370 VFDVMDMLSPLAAQKHIAMAFyyaDNIPQQVIGDALRFKQILTNLISNAIKFTPDGE-IIVRVRMEHDDIGQCllhfsVQ 448
Cdd:PRK09835 342 VGKVFDFFEAWAEERGVELRF---VGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEaITVRCQEVDHQVQLV-----VE 413
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 951237553 449 DSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDN 503
Cdd:PRK09835 414 NPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSD 468
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
666-776 1.96e-21

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: 89.59  E-value: 1.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 666 LAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldgem 745
Cdd:cd00156    1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE------RPDLVLLDLMMPGMDGLELLRKLRELPP------ 68
                         90       100       110
                 ....*....|....*....|....*....|.
gi 951237553 746 QLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd00156   69 DIPVIVLTAKADEEDAVRALELGADDYLVKP 99
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
661-786 6.03e-20

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


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 93.49  E-value: 6.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 661 QGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLESt 740
Cdd:COG2204    1 SMARILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE------PPDLVLLDLRMPGMDGLELLRELRALDP- 73
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 951237553 741 ldgemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:COG2204   74 -----DLPVILLTGYGDVETAVEAIKAGAFDYLTKPFDLEELLAAV 114
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
664-777 6.78e-20

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: 85.96  E-value: 6.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALL---GELNVKTTkaLSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEST 740
Cdd:cd17551    2 RILIVDDNPTNLLLLEALLrsaGYLEVVSF--TDPREALAWCREN------PPDLILLDYMMPGMDGLEFIRRLRALPGL 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 951237553 741 LDgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPI 777
Cdd:cd17551   74 ED----VPIVMITADTDREVRLRALEAGATDFLTKPF 106
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
295-515 9.14e-20

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: 93.64  E-value: 9.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 295 ANISHELRTPLNSIDGFIHLLlrqQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLEletaPFDLEEAVFDVM 374
Cdd:COG5805  292 AGIAHEIRNPLTSIKGFLQLL---QPGIEDKEEYFDIMLSELDRIESIISEFLALAKPQAVNKE----KENINELIQDVV 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 375 DMLSPLAAQKHIAMAFYYADNIPqQVIGDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIgqcllHFSVQDSGIG 453
Cdd:COG5805  365 TLLETEAILHNIQIRLELLDEDP-FIYCDENQIKQVFINLIKNAIEAMPNgGTITIHTEEEDNSV-----IIRVIDEGIG 438
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 951237553 454 LSGTDRKKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQEraptdKGSTF 515
Cdd:COG5805  439 IPEERLKKLGEPF------FTTKEKGTGLGLMVSYKIIENHNGTIDIDSKVG-----KGTTF 489
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
293-498 9.37e-19

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 91.18  E-value: 9.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSIDGFIHlLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLEletaPFDLEEAVFD 372
Cdd:PRK11360 393 LVAGVAHEIRNPLTAIRGYVQ-IWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNALVEE 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 373 VMDMLSPLAAQKHIAMAFYYADNIPQQVIgDALRFKQILTNLISNAIKFTP-DGEIIVRVRMEHDDigqcLLHFSVQDSG 451
Cdd:PRK11360 468 VLQLFQTAGVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQAISaRGKIRIRTWQYSDG----QVAVSIEDNG 542
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 951237553 452 IGLSGTDRKKLFESFSQGDASvtrqfgGTGLGLAISKQLVHLMHGQI 498
Cdd:PRK11360 543 CGIDPELLKKIFDPFFTTKAK------GTGLGLALSQRIINAHGGDI 583
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
299-505 3.99e-18

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 88.36  E-value: 3.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 299 HELRTPLNSIDGFIHLLlrQQNLSNEQ-NLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDML 377
Cdd:PRK11100 265 HELKSPLAAIRGAAELL--QEDPPPEDrARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEAR 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 378 SPLAAQKHIAMAFYYADNipqQVIGDALRFKQILTNLISNAIKFTPDG-EIIVRVRMEHDDIgqcllHFSVQDSGIGLSG 456
Cdd:PRK11100 343 EAQAAAKGITLRLRPDDA---RVLGDPFLLRQALGNLLDNAIDFSPEGgTITLSAEVDGEQV-----ALSVEDQGPGIPD 414
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951237553 457 TDRKKLFESFSqgdaSVTRQFGG---TGLGLAISKQLVHLMHGQIGFEDNQE 505
Cdd:PRK11100 415 YALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPE 462
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
288-498 4.82e-18

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 88.15  E-value: 4.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 288 QAKSVFLANISHELRTPLNSIDGFIHLL---LRQqnLSNEQNLYLQTirkSSAHLLALINDVLDFSKIDAGKLELETAPF 364
Cdd:PRK10549 238 QMRRDFMADISHELRTPLAVLRGELEAIqdgVRK--FTPESVASLQA---EVGTLTKLVDDLHQLSLSDEGALAYRKTPV 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 365 DLEEAVFDVMDMLSPLAAQKHIAMAFYYADNIPqqVIGDALRFKQILTNLISNAIKFTPD-GEIIVRVRMEHDdigQCLL 443
Cdd:PRK10549 313 DLVPLLEVAGGAFRERFASRGLTLQLSLPDSAT--VFGDPDRLMQLFNNLLENSLRYTDSgGSLHISAEQRDK---TLRL 387
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 951237553 444 HFsvQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:PRK10549 388 TF--ADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRI 440
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
665-786 5.98e-18

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


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 80.19  E-value: 5.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldGE 744
Cdd:cd17580    1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRF------RPDVILSDIGMPGMDGYELARRLRELPW---LA 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17580   72 -NTPAIALTGYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
666-776 1.38e-17

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


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 78.60  E-value: 1.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 666 LAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLESTldgem 745
Cdd:cd17574    1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREE------QPDLIILDVMLPGMDGFEVCRRLREKGSD----- 69
                         90       100       110
                 ....*....|....*....|....*....|...
gi 951237553 746 qLPIIALTahALADEKQKL--LKVGMNDYVTKP 776
Cdd:cd17574   70 -IPIIMLT--AKDEEEDKVlgLELGADDYITKP 99
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
289-355 1.47e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 77.61  E-value: 1.47e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553   289 AKSVFLANISHELRTPLNSIDGFIHLLLRqQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAG 355
Cdd:smart00388   1 AKREFLANLSHELRTPLTAIRGYLELLLD-TELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
397-504 1.65e-17

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: 78.99  E-value: 1.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 397 PQQVIGDALRFKQILTNLISNAIKFTPDGEiIVRVRMEHDDIGQcllhFSVQDSGIGLSGTDRKKLFESFSQGDASVTrq 476
Cdd:cd16940    4 DIQVQGDALLLFLLLRNLVDNAVRYSPQGS-RVEIKLSADDGAV----IRVEDNGPGIDEEELEALFERFYRSDGQNY-- 76
                         90       100
                 ....*....|....*....|....*...
gi 951237553 477 fGGTGLGLAISKQLVHLMHGQIGFEDNQ 504
Cdd:cd16940   77 -GGSGLGLSIVKRIVELHGGQIFLGNAQ 103
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
289-355 2.34e-17

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


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 76.87  E-value: 2.34e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553  289 AKSVFLANISHELRTPLNSIDGFIHLLLRQQnLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAG 355
Cdd:pfam00512   1 AKSEFLANLSHELRTPLTAIRGYLELLRDEK-LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
665-776 6.25e-17

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: 77.12  E-value: 6.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELN--VKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStld 742
Cdd:COG4753    2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEH------KPDLVITDINMPGMDGLELLEAIRELDP--- 72
                         90       100       110
                 ....*....|....*....|....*....|....
gi 951237553 743 gemQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:COG4753   73 ---DTKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
403-501 6.25e-17

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: 77.12  E-value: 6.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDIGqclLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGL 482
Cdd:cd16946    1 DRDRLQQLFVNLLENSLRYTDTGGKL-RIRAAQTPQE---VRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                         90
                 ....*....|....*....
gi 951237553 483 GLAISKQLVHLMHGQIGFE 501
Cdd:cd16946   77 GLAICHNIALAHGGTISAE 95
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
287-351 6.57e-17

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 75.71  E-value: 6.57e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951237553 287 NQAKSVFLANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSK 351
Cdd:cd00082    1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEEQREYLERIREEAERLLRLINDLLDLSR 65
PRK10604 PRK10604
sensor protein RstB; Provisional
290-498 2.51e-16

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 82.34  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 290 KSVFLANISHELRTPLnsidgfIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEA 369
Cdd:PRK10604 212 KKQLIDGIAHELRTPL------VRLRYRLEMSDNLSAAESQALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLPAW 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 370 VFDVMDMLSPLAAQKHIAMafyyadNIPQ--QVIGDALR-FKQILTNLISNAIKFTpdgEIIVRVRMEHDDiGQCLLHfs 446
Cdd:PRK10604 286 LSTHLADIQAVTPEKTVRL------DTPHqgDYGALDMRlMERVLDNLLNNALRYA---HSRVRVSLLLDG-NQACLI-- 353
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951237553 447 VQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:PRK10604 354 VEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSV 405
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
278-502 3.09e-16

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 82.29  E-value: 3.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 278 QARDQAISSNQAksvFLANISHELRTPLNSIDGFIHLLLRQQNLSNEqnlyLQTIRKSSAHLLALINDVLDFSKIDAgKL 357
Cdd:PRK09470 234 TALERMMTSQQR---LLSDISHELRTPLTRLQLATALLRRRQGESKE----LERIETEAQRLDSMINDLLVLSRNQQ-KN 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 358 ELETAPFDLEEAVFDVMDMLSPLAAQKHIAMaFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDgEIIVRVRMEHDD 437
Cdd:PRK09470 306 HLERETFKANSLWSEVLEDAKFEAEQMGKSL-TVSAPPGPWPINGNPNALASALENIVRNALRYSHT-KIEVAFSVDKDG 383
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951237553 438 igqclLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFED 502
Cdd:PRK09470 384 -----LTITVDDDGPGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAED 443
envZ PRK09467
osmolarity sensor protein; Provisional
294-498 1.13e-15

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 80.34  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 294 LANISHELRTPLNSIDgfihllLRQQNLSNEQNlYL-QTIRKSSAHLLALINDVLDFSKIDAgklELETAPFDLEEAVFD 372
Cdd:PRK09467 233 MAGVSHDLRTPLTRIR------LATEMMSEEDG-YLaESINKDIEECNAIIEQFIDYLRTGQ---EMPMEMADLNALLGE 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 373 VMdmLSPLAAQKHIAMAFYyadNIPQQVIGDALRFKQILTNLISNAIKFTpDGEIIVRVRMEHDDIGqcllhFSVQDSGI 452
Cdd:PRK09467 303 VI--AAESGYEREIETALQ---PGPIEVPMNPIAIKRALANLVVNAARYG-NGWIKVSSGTEGKRAW-----FQVEDDGP 371
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 951237553 453 GLSGTDRKKLFESFSQGDASvtRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:PRK09467 372 GIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKV 415
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
663-789 1.37e-15

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 74.24  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELN--VKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESt 740
Cdd:COG4565    4 IRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAE------HRPDLILLDIYLPDGDGLELLRELRARGP- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 951237553 741 ldgemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQW 789
Cdd:COG4565   77 -----DVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREALERY 120
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
692-788 3.12e-15

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: 72.76  E-value: 3.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 692 ALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLEStldgemQLPIIALTAHalaDEK---QKLLKVG 768
Cdd:cd17536   31 AENGEEALELIEE-----HKP-DIVITDIRMPGMDGLELIEKIRELYP------DIKIIILSGY---DDFeyaQKAIRLG 95
                         90       100
                 ....*....|....*....|
gi 951237553 769 MNDYVTKPIQMEQIIQILTQ 788
Cdd:cd17536   96 VVDYLLKPVDEEELEEALEK 115
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
665-784 8.59e-15

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: 71.39  E-value: 8.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLpnlIVLEALLGELNVKTT-----KALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLES 739
Cdd:cd17535    1 VLIVDDHP---LVREGLRRLLESEPDievvgEAADGEEALALLREL------RPDVVLMDLSMPGMDGIEALRRLRRRYP 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 951237553 740 tldgemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQ 784
Cdd:cd17535   72 ------DLKVIVLTAHDDPEYVLRALKAGAAGYLLKDSSPEELIE 110
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
411-517 9.19e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 71.08  E-value: 9.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 411 LTNLISNAIKFTPDGEIIvRVRMEHDDIGQcllHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQL 490
Cdd:cd16952    5 FSNLVSNAVKYTPPSDTI-TVRWSQEESGA---RLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLAIVKHV 80
                         90       100
                 ....*....|....*....|....*..
gi 951237553 491 VHLMHGQIGFEdnqerAPTDKGSTFWF 517
Cdd:cd16952   81 MSRHDARLLIA-----SELGKGSRFTC 102
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
664-786 1.47e-14

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: 70.79  E-value: 1.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRslesTLDG 743
Cdd:cd17562    2 KILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQS------KKFDLIITDQNMPNMDGIELIKELR----KLPA 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 951237553 744 EMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17562   72 YKFTPILMLTTESSDEKKQEGKAAGATGWLVKPFDPEQLLEVV 114
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
194-506 2.27e-14

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 75.77  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 194 FYSRRWIA-PMYEIRMQLQRLNADTLDQhIVINSSgelrllQRDIANVVKRLHFSFLELKEhteqteedlrrtldtlevq 272
Cdd:PRK10755  79 FQAVRWITrPLAELQKELEARTADNLTP-IAIHSS------TLEIEAVTSALNQLVSRLTS------------------- 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 273 niTYRQARdqaissnqaksVFLANISHELRTPLNSIDgfIHL-LLRQQNLSNEQNLY--LQTIRKSSAHLLALINDVLDF 349
Cdd:PRK10755 133 --TLDQER-----------LFTADVAHELRTPLAGIR--LHLeLLEKQHHIDVAPLIarLDQMMHTVEQLLQLARAGQSF 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 350 SkidAGKLEletaPFDLEEAVFDVM-DMLSPLAAQKHIAMaFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEII 428
Cdd:PRK10755 198 S---SGHYQ----TVKLLEDVILPSqDELSEMLEQRQQTL-LLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGSTI 269
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553 429 vRVRMEHDDIGqclLHFSVQDSGIGLSGTDRKKLFESFSQGDasvtRQFGGTGLGLAISKQLVHLMHGQIGFEDNQER 506
Cdd:PRK10755 270 -TIKLSQEDGG---AVLAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQNRQER 339
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
663-782 2.39e-14

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 70.12  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQeridQKLKPFDLVFMDIQMPVMSGIDTTRAIRSLEstld 742
Cdd:cd19933    1 LKVLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLA----SAEHSFQLVLLDLCMPEMDGFEVALRIRKLF---- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 951237553 743 GEMQLP-IIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:cd19933   73 GRRERPlIVALTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
665-782 6.81e-14

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: 68.81  E-value: 6.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDQklkpFDLVFMDIQMPVMSGIDTTRAIRSlestldgE 744
Cdd:cd17584    1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDE----FDLVITDVHMPDMDGFEFLELIRL-------E 69
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:cd17584   70 MDLPVIMMSADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
288-497 1.02e-13

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 75.35  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 288 QAKSVFLANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLyLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLE 367
Cdd:PRK10618 448 QARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPE-LDQLAEQSDVLVRLVDNIQLLNMLETQDWKPEQELFSLQ 526
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 368 EAVFDVMDMLSPLAAQKHIAMAFYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVrmEHDDIGQCLLHFSV 447
Cdd:PRK10618 527 DLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEV--DQDESSPDRLTIRI 604
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 448 QDSGIGLSGTDRKKLFESFSqGDASVTRQFGGTGLGLAISKQLVHLMHGQ 497
Cdd:PRK10618 605 LDTGAGVSIKELDNLHFPFL-NQTQGDRYGKASGLTFFLCNQLCRKLGGH 653
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
663-786 1.10e-13

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 71.39  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALL---GELNVKTTkALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLES 739
Cdd:COG3279    2 MKILIVDDEPLARERLERLLekyPDLEVVGE-ASNGEEALELLEE------HKPDLVFLDIQMPGLDGFELARQLRELDP 74
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 740 tldgemQLPIIALTAH---ALadekqKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:COG3279   75 ------PPPIIFTTAYdeyAL-----EAFEVNAVDYLLKPIDEERLAKAL 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
664-783 2.75e-13

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: 67.27  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDg 743
Cdd:cd17618    2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVE------PRPDLILLDWMLPGGSGIQFIRRLKRDEMTRD- 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 744 emqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17618   75 ---IPIIMLTARGEEEDKVRGLEAGADDYITKPFSPRELV 111
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-498 2.82e-13

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: 66.70  E-value: 2.82e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 408 KQILTNLISNAIKFtpdGEIIVRVRMEHDDIGqclLHFSVQDSGIGLSGTDRKKLFESFSQGDASvtRQFGGTGLGLAIS 487
Cdd:cd16950    2 KRVLSNLVDNALRY---GGGWVEVSSDGEGNR---TRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAIV 73
                         90
                 ....*....|.
gi 951237553 488 KQLVHLMHGQI 498
Cdd:cd16950   74 QRISDAHGGSL 84
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
665-783 4.05e-13

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


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 66.64  E-value: 4.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSlestldGE 744
Cdd:cd17627    1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISG------NRPDAVVLDVMMPRLDGLEVCRRLRA------AG 68
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17627   69 NDLPILVLTARDSVSDRVAGLDAGADDYLVKPFALEELL 107
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
660-788 4.74e-13

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 72.37  E-value: 4.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 660 GQGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIdqklkpFDLVFMDIQMPVMSGIDTTRAIRSLES 739
Cdd:PRK10365   3 HDNIDILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQV------FDLVLCDVRMAEMDGIATLKEIKALNP 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 951237553 740 TldgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:PRK10365  77 A------IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
665-786 5.10e-13

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: 66.37  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldge 744
Cdd:cd17550    1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKER------RPDLVLLDIWLPDMDGLELLKEIKEKYP----- 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17550   70 -DLPVIMISGHGTIETAVKATKLGAYDFIEKPLSLDRLLLTI 110
AdeS_HK NF012226
two-component sensor histidine kinase AdeS; Mutations in this component of the two-component ...
285-504 5.45e-13

two-component sensor histidine kinase AdeS; Mutations in this component of the two-component regulatory system for the AdeABC efflux pump can confer adaptive resistance to certain antibiotics, including tigecycline.


Pssm-ID: 411090 [Multi-domain]  Cd Length: 353  Bit Score: 71.56  E-value: 5.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 285 SSNQAKSVFLANISHELRTPLN--------SIDG--------FIHLLLRQQNLSNeqnlylqtirkssahllaLINDVLD 348
Cdd:NF012226 133 SSVKNAQVWNAAIAHELRTPITilqgrlqgILDGvfepdpalFKSLLNQVEGLSH------------------LVEDLRT 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 349 FSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFyyadNIP-QQVIGDALRFKQILTNLISNAIKFTPDGEI 427
Cdd:NF012226 195 LSLVENQQLRLNYESVDLKDSIEKVLKMFEDRLEQAQLTIVL----NLTaTPVFCDRRRIEQVLIALIDNAIRYANAGKL 270
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553 428 IVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQ 504
Cdd:NF012226 271 KISSSVIQDD-----WILQIEDEGPGIAEEYQQDLFNPFFRLEQSRNKEFGGTGLGLAVVHAIVIAHKGSIEYSNSQ 342
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
297-498 5.75e-13

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 73.17  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 297 ISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKidagKLELETAPFDLEEAVFDVMDM 376
Cdd:PRK13837 457 IAHNFNNILGAILGYAEMALNKLARHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPL 532
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 377 LSpLAAQKHIAMAFYYADNiPQQVIGDALRFKQILTNLISNAIK-FTPDGEIIVRVRMEHDDIGQCLLH----------F 445
Cdd:PRK13837 533 LR-VSLPPGVELDFDQDQE-PAVVEGNPAELQQVLMNLCSNAAQaMDGAGRVDISLSRAKLRAPKVLSHgvlppgryvlL 610
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 951237553 446 SVQDSGIGLSGTDRKKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:PRK13837 611 RVSDTGAGIDEAVLPHIFEPF------FTTRAGGTGLGLATVHGIVSAHAGYI 657
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
390-498 9.89e-13

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: 66.00  E-value: 9.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 390 FYYADNIPQQVI---GDALRFKQILTNLISNAIKFTPDGEII-VRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFES 465
Cdd:cd16947    1 FQVEINIPDRPIyanANTEALQRILKNLISNAIKYGSDGKFLgMTLREDEKHV-----YIDIWDKGKGISETEKDHVFER 75
                         90       100       110
                 ....*....|....*....|....*....|...
gi 951237553 466 FSQGDASVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:cd16947   76 LYTLEDSRNSAKQGNGLGLTITKRLAESMGGSI 108
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
295-515 1.03e-12

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 71.36  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 295 ANISHELRTPLNSIDGFIHLLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKidagKLELETAPFDLEEAVFDVM 374
Cdd:PRK10364 242 AGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVK----PTHLALQAVDLNDLINHSL 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 375 DMLSPLAAQKHIAMAFYYADNIPqQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDiGQCLlhfSVQDSGIGL 454
Cdd:PRK10364 318 QLVSQDANSREIQLRFTANDTLP-EIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGA-GVKI---SVTDSGKGI 392
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553 455 SGTDRKKLFesfsqgDASVTRQFGGTGLGLAISKQLVHLMHGQIgfednQERAPTDKGSTF 515
Cdd:PRK10364 393 AADQLEAIF------TPYFTTKAEGTGLGLAVVHNIVEQHGGTI-----QVASQEGKGATF 442
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
155-931 1.48e-12

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 71.62  E-value: 1.48e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 155 VWLLIEMDNQPLELARYRILIALVITGLMTLLLLLLCLNFYSRRWIAPMYEIRMQLQRLNADTLDQHIVINSSGELRLLQ 234
Cdd:COG2198  101 LLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALLLLVLLVLLLL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 235 RDIANVVKRLHFSFLELKEHTEQTEEDLRRTLDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHL 314
Cdd:COG2198  181 LLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLLLLLILLLL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 315 LLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAFYYAD 394
Cdd:COG2198  261 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 395 NIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHDDIGQCLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVT 474
Cdd:COG2198  341 LLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLLLLLLLLLL 420
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 475 RQFGGTGLGLAISKQLVHLMHGQIGFEDNQERAPTDKGSTFWFTAQFAVDEEHEIEHPHFEHLQVVSYLAHPATASVLRY 554
Cdd:COG2198  421 LLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 500
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 555 YLENYQVPHIETQSILDLFSRLKHLDQKDNTWLIVDHSGD-------TEALLKEIRSRYQGNLAVYGYQMTLEPNMLTEY 627
Cdd:COG2198  501 LLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLllllgllALGLAALLLLLALLLGLGLLLGLLLGGLLLLLL 580
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 628 RARPLYQPLSRSGLIQLLSDQPIFEEEQQDFNGQGLHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERID 707
Cdd:COG2198  581 LLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAVLLAAAA 660
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 708 QKLKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDGEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILT 787
Cdd:COG2198  661 AAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLLLLLLLLLL 740
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 788 QWTKNNFTAQNLAKDHHVVAEALDPeilnwqQSLQLAANKEDLAQDLLKMLVDSFPTELEEMQQLIELEDFPQLEHVLHR 867
Cdd:COG2198  741 LLLLLAAAAAAAASPAAPALPVLDL------EALRRLGGDPELLRELLELFLEELPELLAELRQALAAGDLEALARLAHK 814
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 951237553 868 LYGATRYVGTPKLQQVTGDFEQfistlrkerrRADDGFIEEVMRRFDELGLVIKEVESAAHQIL 931
Cdd:COG2198  815 LKGSAGNLGAPRLAELAAELEQ----------AARAGDLEEAEELLAELEAELERVLAALEALL 868
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
210-498 1.74e-12

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 71.26  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 210 LQRLNADTLDQHIVINSSGEL----RLLQRDIANVVKRLHFSFLELKEHtEQTEEDLRRTLDTLevqnityRQARDQAIS 285
Cdd:COG4192  362 MAAIAAGDLDVPIPVDGNDEIgriaRLLRVFRDQAIEKTQELETEIEER-KRIEKNLRQTQDEL-------IQAAKMAVV 433
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 286 SNQAKSVflaniSHELRTPLNSIDGFI---HLLLRQQNLSNEQNlYLQTIRKSSAHLLALINDVLDFSKidagKLELETA 362
Cdd:COG4192  434 GQTMTSL-----AHELNQPLNAMSMYLfsaKKALEQENYAQLPT-SLDKIEGLIERMDKIIKSLRQFSR----KSDTPLQ 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 363 PFDLEEAVFDVMDMLSPLAAQKHIAMafyyadNIPQ--QVIGDALRFKQILTNLISNAIKFTPDGEIIVrVRMEHDDIGQ 440
Cdd:COG4192  504 PVDLRQVIEQAWELVESRAKPQQITL------HIPDdlMVQGDQVLLEQVLVNLLVNALDAVATQPQIS-VDLLSNAENL 576
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553 441 CLlhfSVQDSGIGLSGTDrkKLFESFsqgdasVTRQFGGTGLGLAISKQLVHLMHGQI 498
Cdd:COG4192  577 RV---AISDNGNGWPLVD--KLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDL 623
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
665-786 1.79e-12

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: 64.99  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALL---GELNVKTtkALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLEStl 741
Cdd:cd17542    3 VLIVDDAAFMRMMLKDILtkaGYEVVGE--AANGEEAVEKYKE-----LKP-DLVTMDITMPEMDGIEALKEIKKIDP-- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 951237553 742 dgemQLPIIALTA---HALADEKqklLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17542   73 ----NAKVIMCSAmgqEEMVKEA---IKAGAKDFIVKPFQPERVLEAV 113
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
664-780 1.90e-12

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


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 64.85  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDqklkpFDLVFMDIQMPVMSGIDTTRAIRSLESTldg 743
Cdd:cd17544    2 KVLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPD-----IKLVITDYNMPEMDGFELVREIRKKYSR--- 73
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 951237553 744 eMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQME 780
Cdd:cd17544   74 -DQLAIIGISASGDNALSARFIKAGANDFLTKPFLPE 109
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
213-515 2.29e-12

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 69.88  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 213 LNADTLDQHIVINssGELRLLQRDIANVVKRLHFSFLELKEHTEQteEDLRRTLDTLEVQNITYRQARdqaissnqaksv 292
Cdd:COG3290  134 LETGERDEEILLN--GRVLVVNRVPIRDDGRVVGAVATFRDRTEL--ERLEEELEGVKELAEALRAQR------------ 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 flanisHELRTPLNSIDGFIHLLlRQQNLsneqnlyLQTIRKSSAHLLALINDVLDFSK---IDA---GKLELetapfdl 366
Cdd:COG3290  198 ------HDFRNHLHTISGLLQLG-EYDEA-------LEYIDEISEELQELIDSLLSRIGnpvLAAlllGKAAR------- 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 367 eeavfdvmdmlsplAAQKHIAMAFYYADNIPQQVIGDALrFKQILTNLISNAI---KFTPDGEIIVRVRMEHDDIGqclL 443
Cdd:COG3290  257 --------------ARERGIDLTIDIDSDLPDLPLSDTD-LVTILGNLLDNAIeavEKLPEEERRVELSIRDDGDE---L 318
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951237553 444 HFSVQDSGIGLSGTDRKKLFES-FSqgdasvTRQFGGTGLGLAISKQLVHLMHGQIGFEDNQERaptdkGSTF 515
Cdd:COG3290  319 VIEVEDSGPGIPEELLEKIFERgFS------TKLGEGRGLGLALVKQIVEKYGGTIEVESEEGE-----GTVF 380
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
664-775 2.50e-12

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


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 64.16  E-value: 2.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHlPNLIVL-EALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLEStld 742
Cdd:cd17554    2 KILVVDDE-ENIRELyKEELEDEGYEVVTAGNGEEALEKLES------EDPDLVILDIKMPGMDGLETLRKIREKKP--- 71
                         90       100       110
                 ....*....|....*....|....*....|...
gi 951237553 743 gemQLPIIALTAHalADEKQKLLKVGMNDYVTK 775
Cdd:cd17554   72 ---DLPVIICTAY--SEYKSDFSSWAADAYVVK 99
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
403-504 4.01e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 63.63  E-value: 4.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNAIKFTPDGEII-VRVRMEhddigQCLLHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQfGGTG 481
Cdd:cd16975    1 DTLLLSRALINIISNACQYAPEGGTVsISIYDE-----EEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSG-GHYG 74
                         90       100
                 ....*....|....*....|...
gi 951237553 482 LGLAISKQLVHLMHGQIGFEDNQ 504
Cdd:cd16975   75 MGLYIAKNLVEKHGGSLIIENSQ 97
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-518 6.79e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 62.73  E-value: 6.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNAIKFTPDGEiIVRVRMEHDDIGQCLLhFSVQDSGIGLSGTDRKKLFESF----SQGDasvtrqFGGTGLGL 484
Cdd:cd16921    3 QVLTNLLGNAIKFRRPRR-PPRIEVGAEDVGEEWT-FYVRDNGIGIDPEYAEKVFGIFqrlhSREE------YEGTGVGL 74
                         90       100       110
                 ....*....|....*....|....*....|....
gi 951237553 485 AISKQLVHLMHGQIGFEdnqerAPTDKGSTFWFT 518
Cdd:cd16921   75 AIVRKIIERHGGRIWLE-----SEPGEGTTFYFT 103
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
663-788 9.44e-12

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: 62.74  E-value: 9.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVK-TTKALSGQEALniiqeridQKLKP--FDLVFMDIQMPVMSGIDTTRAIRSles 739
Cdd:cd19923    1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDAL--------EKLKAggFDFVITDWNMPNMDGLELLKTIRA--- 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 740 tlDGEMQ-LPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd19923   70 --DGALShLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEK 117
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
665-782 1.28e-11

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 67.95  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIqeridqKLKPFDLVFMDIQMPVMSGIDTTRAIRSLEStldge 744
Cdd:PRK11361   7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLF------ADIHPDVVLMDIRMPEMDGIKALKEMRSHET----- 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:PRK11361  76 -RTPVILMTAYAEVETAVEALRCGAFDYVIKPFDLDEL 112
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-518 1.59e-11

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: 61.64  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 408 KQILTNLISNAIKFTPDGEIIVR---VRMEHDDIGQclLHFSVQDSGIGLSGTDRKKLFESFsqgdasVTRQFGGTGLGL 484
Cdd:cd16920    2 QQVLINLVRNGIEAMSEGGCERReltIRTSPADDRA--VTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLGMGL 73
                         90       100       110
                 ....*....|....*....|....*....|....
gi 951237553 485 AISKQLVHLMHGQIGFEDNQERaptdkGSTFWFT 518
Cdd:cd16920   74 SICRSIIEAHGGRLSVESPAGG-----GATFQFT 102
PRK09303 PRK09303
histidine kinase;
247-518 1.61e-11

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 67.28  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 247 SFLELKEHTEQTEEDLRRT---LDTLEVQNITYRQARDQAISSNQAKSVFLANISHELRTPLNSIDGFIHLL-LRQQNLS 322
Cdd:PRK09303 105 TYSGLGENLQPSEIDSGRYsqeLLQLSDELFVLRQENETLLEQLKFKDRVLAMLAHDLRTPLTAASLALETLeLGQIDED 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 323 NEQNLYLQT-----IRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEEAVFDVMDMLSPLAAQKHIAMAfyyADnIP 397
Cdd:PRK09303 185 TELKPALIEqlqdqARRQLEEIERLITDLLEVGRTRWEALRFNPQKLDLGSLCQEVILELEKRWLAKSLEIQ---TD-IP 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 398 QQ---VIGDALRFKQILTNLISNAIKFTPDGEIIvRVRMehddigqclLH-------FSVQDSGIGLSGTDRKKLFE-SF 466
Cdd:PRK09303 261 SDlpsVYADQERIRQVLLNLLDNAIKYTPEGGTI-TLSM---------LHrttqkvqVSICDTGPGIPEEEQERIFEdRV 330
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 951237553 467 S-QGDASVTrqfgGTGLGLAISKQLVHLMHGQIGFEDNqerapTDKGSTFWFT 518
Cdd:PRK09303 331 RlPRDEGTE----GYGIGLSVCRRIVRVHYGQIWVDSE-----PGQGSCFHFT 374
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
666-777 2.25e-11

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: 61.52  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 666 LAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLdgem 745
Cdd:cd19937    1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKD------EKPDLIILDLMLPGIDGLEVCRILRSDPKTS---- 70
                         90       100       110
                 ....*....|....*....|....*....|....
gi 951237553 746 QLPIIALTAHalADEKQKL--LKVGMNDYVTKPI 777
Cdd:cd19937   71 SIPIIMLTAK--GEEFDKVlgLELGADDYITKPF 102
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
665-776 2.28e-11

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: 61.63  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDQKL---KPFDLVFMDIQMPVMSGIDTTRAIRSlestl 741
Cdd:cd19924    1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKEGNdlsKELDLIITDIEMPKMDGYELTFELRD----- 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 951237553 742 DGEMQ-LPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd19924   76 DPRLAnIPVILNSSLSGEFSRARGKKVGADAYLAKF 111
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
407-503 3.11e-11

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: 60.80  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 407 FKQILTNLISNAIKFTPdGEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAI 486
Cdd:cd16949    1 LARALENVLRNALRYSP-SKILLDISQDGDQW-----TITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                         90
                 ....*....|....*..
gi 951237553 487 SKQLVHLMHGQIGFEDN 503
Cdd:cd16949   75 AERAIEQHGGKIKASNR 91
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
664-788 6.37e-11

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: 60.89  E-value: 6.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHlPN--LIVLEALL-GELNVKTTKALSGQEALNIIQERIDQKLKPF-DLVFMDIQMPVMSGIDTTRAIRSLES 739
Cdd:cd17557    1 TILLVEDN-PGdaELIQEAFKeAGVPNELHVVRDGEEALDFLRGEGEYADAPRpDLILLDLNMPRMDGFEVLREIKADPD 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 951237553 740 TldgeMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd17557   80 L----RRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIRS 124
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
403-506 6.88e-11

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 59.86  E-value: 6.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNA---IKFTPDGEIIVRVRMEHDDIGQCLLhfSVQDSGIGLSGTDRKKLFESFsqgdasVTRQFGG 479
Cdd:cd16944    1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRVEADQDGRIVL--IVCDNGKGFPREMRHRATEPY------VTTRPKG 72
                         90       100
                 ....*....|....*....|....*..
gi 951237553 480 TGLGLAISKQLVHLMHGQIGFEDNQER 506
Cdd:cd16944   73 TGLGLAIVKKIMEEHGGRISLSNREAG 99
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
665-783 8.49e-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: 60.06  E-value: 8.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHlPNLIVLEAL-LGELNVKTTKALSGQEALniiqeRIDQKLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldG 743
Cdd:cd17615    2 VLVVDDE-PNITELLSMaLRYEGWDVETAADGAEAL-----AAAREFRP-DAVVLDIMLPDMDGLEVLRRLRA------D 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 744 EMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17615   69 GPDVPVLFLTAKDSVEDRIAGLTAGGDDYVTKPFSLEEVV 108
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
665-783 9.01e-11

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


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 59.74  E-value: 9.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLESTldge 744
Cdd:cd17614    1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEE-----EQP-DLILLDLMLPEKDGLEVCREVRKTSNV---- 70
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 mqlPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17614   71 ---PIIMLTAKDSEVDKVLGLELGADDYVTKPFSNRELL 106
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
692-776 1.24e-10

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


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 59.71  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 692 ALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldgEMQLPIIALTAHALADEKQ--KLLKVGM 769
Cdd:cd17541   32 ARDGEEALEKIKE-----LKP-DVITLDIEMPVMDGLEALRRIMA-------ERPTPVVMVSSLTEEGAEItlEALELGA 98

                 ....*..
gi 951237553 770 NDYVTKP 776
Cdd:cd17541   99 VDFIAKP 105
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
293-505 1.40e-10

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


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 65.15  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  293 FLANISHELRTPL----NSIDgfihlLLRQQNLSNEQNLYLQTIRKSSAHLLALINDVLDFSKIDAGKLELETAPFDLEE 368
Cdd:TIGR03785 488 MSSRLSHELRTPVavvrSSLE-----NLELQALEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSE 562
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  369 AVFDVMDMLSPLAAQKHIAmafYYADNIPQQVIGDALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDiGQCLLhfSVQ 448
Cdd:TIGR03785 563 VLSGCMQGYQMTYPPQRFE---LNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGLI-EVGLSQNK-SHALL--TVS 635
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553  449 DSGIGLSGTDRKKLFESF-SQGDASVTRQfGGTGLGLAISKQLVHLMHGQIGFEDNQE 505
Cdd:TIGR03785 636 NEGPPLPEDMGEQLFDSMvSVRDQGAQDQ-PHLGLGLYIVRLIADFHQGRIQAENRQQ 692
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
408-515 1.59e-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: 58.97  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 408 KQILTNLISNAIK-FTPDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFESFSqgdasVTRQFG-GTGLGLA 485
Cdd:cd16943    5 NQVLLNLLVNAAQaMEGRGRITIRTWAHVDQ-----VLIEVEDTGSGIDPEILGRIFDPFF-----TTKPVGeGTGLGLS 74
                         90       100       110
                 ....*....|....*....|....*....|
gi 951237553 486 ISKQLVHLMHGQIgfednQERAPTDKGSTF 515
Cdd:cd16943   75 LSYRIIQKHGGTI-----RVASVPGGGTRF 99
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
665-776 2.26e-10

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 58.33  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEstldge 744
Cdd:cd17620    1 ILVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATR------KPDLIILDLGLPDMDGLEVIRRLREWS------ 68
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd17620   69 -AVPVIVLSARDEESDKIAALDAGADDYLTKP 99
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
664-786 6.84e-10

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


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 57.56  E-value: 6.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHlPNL-----IVLEaLLGELNVKTtkALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSLE 738
Cdd:cd17552    3 RILVIDDE-EDIrevvqACLE-KLAGWEVLT--ASSGQEGLEKAATE-----QP-DAILLDVMMPDMDGLATLKKLQANP 72
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951237553 739 STldgeMQLPIIALTAHALADEKQKLLKVGMNDYVTKP---IQM-EQIIQIL 786
Cdd:cd17552   73 ET----QSIPVILLTAKAQPSDRQRFASLGVAGVIAKPfdpLTLaEQIAKLL 120
pleD PRK09581
response regulator PleD; Reviewed
665-777 7.76e-10

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 62.23  E-value: 7.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEA-LLGE-LNVKTtkALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTld 742
Cdd:PRK09581   5 ILVVDDIPANVKLLEAkLLAEyYTVLT--ASSGAEAIAICER------EQPDIILLDVMMPGMDGFEVCRRLKSDPAT-- 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 743 geMQLPIIALTAHALADEKQKLLKVGMNDYVTKPI 777
Cdd:PRK09581  75 --THIPVVMVTALDDPEDRVRGLEAGADDFLTKPI 107
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
665-783 8.18e-10

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


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 57.29  E-value: 8.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLdge 744
Cdd:cd19934    1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEE------EPYDLVVLDLGLPGMDGLSVLRRWRSEGRAT--- 71
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 mqlPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd19934   72 ---PVLILTARDSWQDKVEGLDAGADDYLTKPFHIEELL 107
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
661-786 1.16e-09

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: 58.81  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 661 QGLHILAVDDHLPNLIVLEALLGELNVK-TTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRsles 739
Cdd:COG3707    2 RGLRVLVVDDEPLRRADLREGLREAGYEvVAEAADGEDAVELVRE-----LKP-DLVIVDIDMPDRDGLEAARQIS---- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 951237553 740 tldGEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:COG3707   72 ---EERPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPAL 115
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
665-783 1.57e-09

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


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 56.44  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAI--RSLEStld 742
Cdd:cd17572    1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSD------QPPDVVLLDLKLPDMSGMEILKWIqeRSLPT--- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 951237553 743 gemqlPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17572   72 -----SVIVITAHGSVDIAVEAMRLGAYDFLEKPFDADRLR 107
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
665-776 1.72e-09

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


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 55.62  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSlestldGE 744
Cdd:cd19926    1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASE------PYDLCLTDMRLPDGSGLELVQHIQQ------RL 68
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd19926   69 PQTPVAVITAYGSLDTAIEALKAGAFDFLTKP 100
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
833-916 1.77e-09

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


Pssm-ID: 426352 [Multi-domain]  Cd Length: 84  Bit Score: 55.05  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  833 DLLKMLVDSFPTELEEMQQLIELEDFPQLEHVLHRLYGATRYVGTPKLQQVTGDFEQFistLRKERRRADDGFIEEVMRR 912
Cdd:pfam01627   1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDL---LREGELPLDPELLEALRDL 77

                  ....
gi 951237553  913 FDEL 916
Cdd:pfam01627  78 LEAL 81
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
411-504 2.72e-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: 55.51  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 411 LTNLISNAIKFTPDgeiivRVRMEH-DDIGQCLLhfSVQDSGIGLSGTDRKKLFESFSQGDASVTRQFGGTGLGLAISKQ 489
Cdd:cd16939    5 LDNLLRNALRYAHR-----TVRIALlVSGGRLTL--IVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAIVHR 77
                         90
                 ....*....|....*
gi 951237553 490 LVHLMHGQIGFEDNQ 504
Cdd:cd16939   78 VALWHGGHVECDDSE 92
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-501 3.06e-09

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


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 55.48  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNAIKFTP--DGEIIVRVRMEHddigQCLLH---------FSVQDSGIGLSGTDRKKLFESFsqgdasVTRQF 477
Cdd:cd16918    3 QVFLNLVRNAAQALAgsGGEIILRTRTQR----QVTLGhprhrlalrVSVIDNGPGIPPDLQDTIFYPM------VSGRE 72
                         90       100
                 ....*....|....*....|....
gi 951237553 478 GGTGLGLAISKQLVHLMHGQIGFE 501
Cdd:cd16918   73 NGTGLGLAIAQNIVSQHGGVIECD 96
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
665-782 3.23e-09

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: 55.49  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDhlpNLIV---LEALLGELNVKTTK-ALSGQEALNIIQEridqkLKPfDLVFMDIQMP-VMSGIDTTRAIRSles 739
Cdd:cd17534    3 ILIVED---EAIIaldLKEILESLGYEVVGiADSGEEAIELAEE-----NKP-DLILMDINLKgDMDGIEAAREIRE--- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 951237553 740 tldgEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:cd17534   71 ----KFDIPVIFLTAYSDEETLERAKETNPYGYLVKPFNEREL 109
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-515 4.71e-09

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: 54.89  E-value: 4.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNAIKFTPD--GEIIVRVRMEHDdigqcLLHFSVQDSGIGLSGTDRKKLFESF-SQGDASvtRQFG-GTGLGL 484
Cdd:cd16953    3 QVLRNLIGNAISFSPPdtGRITVSAMPTGK-----MVTISVEDEGPGIPQEKLESIFDRFyTERPAN--EAFGqHSGLGL 75
                         90       100       110
                 ....*....|....*....|....*....|.
gi 951237553 485 AISKQLVHLmHGQIGFEDNQERAPTDKGSTF 515
Cdd:cd16953   76 SISRQIIEA-HGGISVAENHNQPGQVIGARF 105
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
664-783 6.24e-09

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


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 54.70  E-value: 6.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSlestldg 743
Cdd:cd17619    2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR------QDIDLVLLDINLPGKDGLSLTRELRE------- 68
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 744 EMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17619   69 QSEVGIILVTGRDDEVDRIVGLEIGADDYVTKPFNPRELL 108
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
410-515 1.22e-08

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


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 53.54  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 410 ILTNLISNAIKFTPDGeiiVRVRMEHDDIGQCLlhfSVQDSGIGLSGTDRK--KLFESFSQGDASvtRQFGGTGLGLAIS 487
Cdd:cd16923    4 VFSNLLSNAIKYSPEN---TRIYITSFLTDDVV---NIMFKNPSSHPLDFKleKLFERFYRGDNS--RNTEGAGLGLSIA 75
                         90       100
                 ....*....|....*....|....*...
gi 951237553 488 KQLVHLMHGQIGFEDNqeraptDKGSTF 515
Cdd:cd16923   76 KAIIELHGGSASAEYD------DNHDLF 97
resp_reg_YycF NF040534
response regulator YycF;
665-783 1.23e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 56.65  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldgE 744
Cdd:NF040534   3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEE-----EVP-DLVLLDIMLPGRDGMEVCREVRK-------K 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:NF040534  70 YDMPIIMLTAKDSEIDKVLGLELGADDYVTKPFSTRELI 108
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
663-789 2.01e-08

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: 53.40  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDhlpnlivlEALLGELNVKTTKAL----------SGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTR 732
Cdd:cd19925    1 INVLIVED--------DPMVAEIHRAYVEQVpgftvigtagTGEEALKLLKER------QPDLILLDIYLPDGNGLDLLR 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553 733 AIRSLESTLDgemqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQW 789
Cdd:cd19925   67 ELRAAGHDVD------VIVVTAANDVETVREALRLGVVDYLIKPFTFERLRQRLERY 117
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
677-788 2.02e-08

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: 53.31  E-value: 2.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 677 VLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTtrairsLESTLDGEMQLPIIALTAHA 756
Cdd:cd17593   16 LARALPADWDVEITFAENGEEALEILRE------GRIDVLFLDLTMPVMDGYEV------LEALPVEQLETKVIVVSGDV 83
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 757 LADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd17593   84 QPEAKERVLELGALAFLKKPFDPEKLAQLLEE 115
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
665-788 2.10e-08

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: 53.10  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd17598    1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEH-----RP-TLVISDIVMPEMDGYELCRKIKSDPDLKD-- 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 951237553 745 mqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQ----MEQIIQILTQ 788
Cdd:cd17598   73 --IPVILLTTLSDPRDVIRGLECGADNFITKPYDekylLSRIKYILVN 118
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
663-723 2.13e-08

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 51.03  E-value: 2.13e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553   663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMP 723
Cdd:smart00448   1 MRILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKE------EKPDLILLDIMMP 55
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
665-788 2.55e-08

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 52.79  E-value: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSL-ESTLDg 743
Cdd:cd17569    3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQE------PVDVVISDQRMPGMDGAELLKRVRERyPDTVR- 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 744 emqlpiIALTAHAladEKQKLLKVgMND-----YVTKPIQMEQIIQILTQ 788
Cdd:cd17569   76 ------ILLTGYA---DLDAAIEA-INEgeiyrFLTKPWDDEELKETIRQ 115
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
665-786 2.96e-08

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: 52.93  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTT--KALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLEstld 742
Cdd:cd17532    1 ALIVDDEPLAREELRYLLEEHPDIEIvgEAENGEEALEAIEE-----LKP-DVVFLDIQMPGLDGLELAKKLSKLA---- 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 951237553 743 gemQLP-IIALTAH---ALadekqKLLKVGMNDYVTKPIQMEQIIQIL 786
Cdd:cd17532   71 ---KPPlIVFVTAYdeyAV-----EAFELNAVDYLLKPFSEERLAEAL 110
orf27 CHL00148
Ycf27; Reviewed
664-776 3.65e-08

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 55.11  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQeridqKLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldg 743
Cdd:CHL00148   8 KILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFR-----KEQP-DLVILDVMMPKLDGYGVCQEIRK------- 74
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 744 EMQLPIIALTAhaLADEKQKL--LKVGMNDYVTKP 776
Cdd:CHL00148  75 ESDVPIIMLTA--LGDVSDRItgLELGADDYVVKP 107
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
666-783 6.04e-08

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


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 51.84  E-value: 6.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 666 LAVDD--HLPNLIVleALLGELNVKTTKALSGQEALNIIQERIdqklkpFDLVFMDIQMPVMSGIDTTRAIRslestlDG 743
Cdd:cd17625    1 LVVEDekDLSEAIT--KHLKKEGYTVDVCFDGEEGLEYALSGI------YDLIILDIMLPGMDGLEVLKSLR------EE 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 744 EMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17625   67 GIETPVLLLTALDAVEDRVKGLDLGADDYLPKPFSLAELL 106
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
691-783 6.63e-08

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: 51.65  E-value: 6.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 691 KALSGQEALNIIQeridqKLKPfDLVFMDIQMPVMSGIDTTRAIRslestldGEMQLPIIALTAHALADEKQKLLKVGMN 770
Cdd:cd19932   30 EASDGEEAVELAK-----KHKP-DLVIMDVKMPRLDGIEAAKIIT-------SENIAPIVLLTAYSQQDLVERAKEAGAM 96
                         90
                 ....*....|...
gi 951237553 771 DYVTKPIQMEQII 783
Cdd:cd19932   97 AYLVKPFSESDLI 109
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
665-802 8.72e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 54.04  E-value: 8.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDqklkpfdLVFMDIQMPVMSGIDTTRAIRSlestldgE 744
Cdd:PRK10955   4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDDSID-------LLLLDVMMPKKNGIDTLKELRQ-------T 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPI-QMEQIIQILTQWTKNNFTAQNLAKD 802
Cdd:PRK10955  70 HQTPVIMLTARGSELDRVLGLELGADDYLPKPFnDRELVARIRAILRRSHWSEQQQNND 128
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
405-490 9.49e-08

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: 51.13  E-value: 9.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 405 LRFkqILTNLISNAIKFTPDGEIIVrVRMEHDDIGQCLlhfSVQDSGIGLSGTDRKKLFESFSQGdaSVTRQFG-GTGLG 483
Cdd:cd16948    6 LSF--IIGQIVSNALKYSKQGGKIE-IYSETNEQGVVL---SIKDFGIGIPEEDLPRVFDKGFTG--ENGRNFQeSTGMG 77

                 ....*..
gi 951237553 484 LAISKQL 490
Cdd:cd16948   78 LYLVKKL 84
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
692-778 9.90e-08

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


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 51.05  E-value: 9.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 692 ALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLestldgEMQLPIIALTAHALADEKQKLLKVGMND 771
Cdd:cd17555   30 AADGRQGLELFRS------EQPDLVLCDLRMPEMDGLEVLKQITKE------SPDTPVIVVSGAGVMSDAVEALRLGAWD 97

                 ....*..
gi 951237553 772 YVTKPIQ 778
Cdd:cd17555   98 YLTKPIE 104
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
403-498 1.12e-07

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 50.92  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNAIKFTPDGEIIvRVRMEHDDIGQCLLhfsVQDSGIGLSGTDRKKLFESFSqgdaSVTRQFGG--- 479
Cdd:cd16945    1 DPFLLRQAINNLLDNAIDFSPEGGLI-ALQLEADTEGIELL---VFDEGSGIPDYALNRVFERFY----SLPRPHSGqks 72
                         90
                 ....*....|....*....
gi 951237553 480 TGLGLAISKQLVHLMHGQI 498
Cdd:cd16945   73 TGLGLAFVQEVAQLHGGRI 91
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
665-780 1.34e-07

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


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 50.95  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLpnLIV--LEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSlestld 742
Cdd:cd17624    1 ILLVEDDA--LLGdgLKTGLRKAGYAVDWVRTGAEAEAALASG------PYDLVILDLGLPDGDGLDLLRRWRR------ 66
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 743 GEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQME 780
Cdd:cd17624   67 QGQSLPVLILTARDGVDDRVAGLDAGADDYLVKPFALE 104
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
695-776 1.89e-07

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 53.04  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 695 GQEALniiqERIDQKlkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldgemQLPIIALTAHalADEKQKL--LKVGMNDY 772
Cdd:PRK11083  36 GLPAL----DKLRQQ--PPDLVILDVGLPDISGFELCRQLLAFHP------ALPVIFLTAR--SDEVDRLvgLEIGADDY 101

                 ....
gi 951237553 773 VTKP 776
Cdd:PRK11083 102 VAKP 105
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
665-783 3.12e-07

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: 49.72  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIiqeridQKLKPFDLVFMDIQMPVMSGIDTTRAIRSlestldGE 744
Cdd:cd17616    1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDL------GKLYDYDIILLDLNLPDMSGYEVLRTLRL------AK 68
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17616   69 VKTPILILSGLADIEDKVKGLGFGADDYMTKPFHKDELV 107
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
695-776 3.29e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 53.62  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 695 GQEALNIIQeridqKLKPfDLVFMDIQMPVMSGIDTTRAIrslestldgeMQL---PII---ALTaHALADEKQKLLKVG 768
Cdd:PRK00742  38 GLEAREKIK-----KLNP-DVITLDVEMPVMDGLDALEKI----------MRLrptPVVmvsSLT-ERGAEITLRALELG 100

                 ....*...
gi 951237553 769 MNDYVTKP 776
Cdd:PRK00742 101 AVDFVTKP 108
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
665-776 3.59e-07

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: 48.98  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEstldge 744
Cdd:cd19935    1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTN------EYDLIILDVMLPGLDGLEVLRRLRAAG------ 68
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd19935   69 KQTPVLMLTARDSVEDRVKGLDLGADDYLVKP 100
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
410-503 4.01e-07

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


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 49.21  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 410 ILTNLISNAI-----KFTPDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFES-FSqgdasvTRQFGGTGLG 483
Cdd:cd16915    4 IVGNLIDNALdalaaTGAPNKQVEVFLRDEGDD-----LVIEVRDTGPGIAPELRDKVFERgVS------TKGQGERGIG 72
                         90       100
                 ....*....|....*....|
gi 951237553 484 LAISKQLVHLMHGQIGFEDN 503
Cdd:cd16915   73 LALVRQSVERLGGSITVESE 92
PRK10610 PRK10610
chemotaxis protein CheY;
663-776 5.67e-07

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 49.59  E-value: 5.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGEL---NVKttKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSles 739
Cdd:PRK10610   6 LKFLVVDDFSTMRRIVRNLLKELgfnNVE--EAEDGVDALNKLQA------GGFGFVISDWNMPNMDGLELLKTIRA--- 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 740 tlDGEM-QLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:PRK10610  75 --DGAMsALPVLMVTAEAKKENIIAAAQAGASGYVVKP 110
PRK10337 PRK10337
sensor protein QseC; Provisional
293-505 6.57e-07

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 52.73  E-value: 6.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 293 FLANISHELRTPLNSidgfihllLRQQ----NLSNEQnlyLQTIRKSSAHLLA-------LINDVLDFSKIDAGKLELET 361
Cdd:PRK10337 240 FTSDAAHELRSPLAA--------LKVQtevaQLSDDD---PQARKKALLQLHAgidratrLVDQLLTLSRLDSLDNLQDV 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 362 APFDLEEAVFD-VMDMLSPlAAQKHIAMAFYY-ADNIPQQviGDALRFKQILTNLISNAIKFTPDGEIIVRVRMEHddig 439
Cdd:PRK10337 309 AEIPLEDLLQSaVMDIYHT-AQQAGIDVRLTLnAHPVIRT--GQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNAR---- 381
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 951237553 440 qcllHFSVQDSGIGLSGTDRKKLFESFSQ---GDASvtrqfgGTGLGLAISKQLVHLMHGQIGFeDNQE 505
Cdd:PRK10337 382 ----NFTVRDNGPGVTPEALARIGERFYRppgQEAT------GSGLGLSIVRRIAKLHGMNVSF-GNAP 439
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
665-782 8.06e-07

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: 48.70  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd17553    3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTK------ERPDLVLLDMKIPGMDGIEILKRMKVIDENIR-- 74
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 745 mqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:cd17553   75 ----VIIMTAYGELDMIQESKELGALTHFAKPFDIDEI 108
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
665-776 1.10e-06

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: 48.07  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHlpnlIVLEALLGEL------NVKTtkALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSle 738
Cdd:cd17623    1 ILLIDDD----RELTELLTEYlemegfNVRA--AHDGEQGLAALLE------GSPDLVVLDVMLPKMNGLDVLKELRK-- 66
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 739 stldgEMQLPIIALTAHalADEKQKL--LKVGMNDYVTKP 776
Cdd:cd17623   67 -----TSQVPVLMLTAR--GDDIDRIlgLELGADDYLPKP 99
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
665-779 1.27e-06

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: 48.13  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDQKLKPF-----DLVFMDIQMPVMSGIDTTRAIRSLeS 739
Cdd:cd17581    1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDSSNFnepkvNMIITDYCMPGMTGYDLLKKVKES-S 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 740 TLDgemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQM 779
Cdd:cd17581   80 ALK---EIPVVIMSSENIPTRISRCLEEGAEDFLLKPVKL 116
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
665-776 1.31e-06

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 47.88  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklKPFDLVFMDIQMPVMSGIDTTRAIRSLEStldge 744
Cdd:cd18160    2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQG-----KDIDIVVTDIVMPEMDGIELAREARKIDP----- 71
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 mQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd18160   72 -DVKILFISGGAAAAPELLSDAVGDNATLKKP 102
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
665-783 1.43e-06

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: 47.85  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSlestldgE 744
Cdd:cd17626    3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFRE-----VRP-DLVLLDLMLPGIDGIEVCRQIRA-------E 69
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:cd17626   70 SGVPIVMLTAKSDTVDVVLGLESGADDYVAKPFKPKELV 108
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
665-776 1.70e-06

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


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 47.19  E-value: 1.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALniiqERIDQKlkPFDLVFMDIQMPVMSGIDTTRAIRslestldGE 744
Cdd:cd17621    1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAAL----AEFDRA--GADIVLLDLMLPGLSGTEVCRQLR-------AR 67
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 MQLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd17621   68 SNVPVIMVTAKDSEIDKVVGLELGADDYVTKP 99
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
665-788 2.32e-06

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 49.64  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDH------LPNLIVLEA---LLGElnvkttkALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIR 735
Cdd:PRK10651   9 ILLIDDHpmlrtgVKQLISMAPditVVGE-------ASNGEQGIELAES-----LDP-DLILLDLNMPGMNGLETLDKLR 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 951237553 736 slESTLDGEmqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:PRK10651  76 --EKSLSGR----IVVFSVSNHEEDVVTALKRGADGYLLKDMEPEDLLKALQQ 122
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
665-788 2.45e-06

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


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 47.34  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDH------LPNLIVLE---ALLGElnvkttkALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIR 735
Cdd:cd19931    1 VLLIDDHpllrkgIKQLIELDpdfTVVGE-------ASSGEEGIELAER-----LDP-DLILLDLNMKGMSGLDTLKALR 67
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 951237553 736 slESTLDGEmqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd19931   68 --EEGVSAR----IVILTVSDAEDDVVTALRAGADGYLLKDMEPEDLLEALKQ 114
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
663-734 2.71e-06

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: 47.58  E-value: 2.71e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553 663 LHILAVDDHLpnlIVLEALLGELNVKT-----TKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAI 734
Cdd:COG2197    2 IRVLIVDDHP---LVREGLRALLEAEPdievvGEAADGEEALELLEE------LRPDVVLLDIRMPGMDGLEALRRL 69
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
664-776 3.34e-06

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: 46.99  E-value: 3.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldg 743
Cdd:cd19938    1 RILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHT------PPDLILLDLMLPGTDGLTLCREIRRFSD---- 70
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 744 emqLPIIALTAHalADEKQKL--LKVGMNDYVTKP 776
Cdd:cd19938   71 ---VPIIMVTAR--VEEIDRLlgLELGADDYICKP 100
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
665-776 3.51e-06

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: 46.57  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDqklkpFDLVFMDIQMP-VMSG---IDTTRAIRSlest 740
Cdd:cd18161    1 VLVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGPD-----IDLLVTDVIMPgGMNGsqlAEEARRRRP---- 71
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 951237553 741 ldgemQLPIIALTAHALADEKQKLLKVGMnDYVTKP 776
Cdd:cd18161   72 -----DLKVLLTSGYAENAIEGGDLAPGV-DVLSKP 101
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
664-776 3.96e-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: 46.67  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSG-QEALNIIQERIDqklkpfdLVFMDIQMPVMSGIDTTRAIRSlestld 742
Cdd:cd17594    1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGaEEARLMLHRRVD-------LVLLDLRLGQESGLDLLRTIRA------ 67
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 951237553 743 gEMQLPIIALTAHALaDEKQKL--LKVGMNDYVTKP 776
Cdd:cd17594   68 -RSDVPIIIISGDRR-DEIDRVvgLELGADDYLAKP 101
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
402-521 4.79e-06

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


Pssm-ID: 340409 [Multi-domain]  Cd Length: 113  Bit Score: 46.50  E-value: 4.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 402 GDALRFKQILTNLISNAIKFTP--DG--EIIVRVRMEHDDIGQCLLH--FSVQDSGIGLSgtdrKKLFESFSQGDASVTR 475
Cdd:cd16932    2 GDQIRLQQVLADFLLNAVRFTPspGGwvEIKVSPTKKQIGDGVHVIHleFRITHPGQGLP----EELVQEMFEENQWTTQ 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 951237553 476 QfggtGLGLAISKQLVHLMHGQIGFEDNQERaptdkgSTFWFTAQF 521
Cdd:cd16932   78 E----GLGLSISRKLVKLMNGDVRYLREAGR------SYFLITLEL 113
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
665-776 6.28e-06

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: 45.83  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDD--HLPNLIVLEALLGELNVKTtkALSGQEALNIIqeridqKLKPFDLVFMDIQMPVMSGIDTTRAIRSlestlD 742
Cdd:cd19927    1 ILLVDDdpGIRLAVKDYLEDQGFTVIA--ASNGLEALDLL------NQYIPDLIISDIIMPGVDGYSLLGKLRK-----N 67
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 743 GEMQ-LPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd19927   68 ADFDtIPVIFLTAKGMTSDRIKGYNAGCDGYLSKP 102
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
664-778 8.79e-06

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 45.83  E-value: 8.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSlestldg 743
Cdd:cd19939    1 RILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDE-----QP-SLVVLDIMLPGMDGLTVCREVRE------- 67
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 951237553 744 EMQLPIIALTAHalADEKQKLL--KVGMNDYVTKPIQ 778
Cdd:cd19939   68 HSHVPILMLTAR--TEEMDRVLglEMGADDYLCKPFS 102
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
396-509 9.44e-06

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: 45.91  E-value: 9.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 396 IPQQVIGDALRFKQILTNLISNAIKFT-PDGEIIVRVRMEHDDIGQCLLH----------------FSVQDSGIGLSGTD 458
Cdd:cd16938    1 LPDVVVGDERRVFQVLLHMLGNLLKMRnGGGNITFRVFLEGGSEDRSDRDwgpwrpsmsdesveirFEVEINDSGSPSIE 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 951237553 459 RKKLFESFSQGDASVTRqfgGTGLGLAISKQLVHLMHGQIGFEDNQERAPT 509
Cdd:cd16938   81 SASMRNSLNRRYNLSEL---GEHLSFSICKQLVQLMGGNIWIVPGSGLGTT 128
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
677-785 1.04e-05

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: 45.34  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 677 VLEALLGELNVKTTKALSGQEALNIIQeridqKLKPfDLVFMDIQMPVMSGIDTTRAIRSLEStldgemQLPIIALTAHA 756
Cdd:cd19919   15 VLERALAGAGLTVTSFENAQEALAALA-----SSQP-DVLISDIRMPGMDGLALLAQIKQRHP------DLPVIIMTAHS 82
                         90       100
                 ....*....|....*....|....*....
gi 951237553 757 LADEKQKLLKVGMNDYVTKPIQMEQIIQI 785
Cdd:cd19919   83 DLDSAVSAYQGGAFEYLPKPFDIDEAVAL 111
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
695-776 1.05e-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: 45.13  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 695 GQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSlestldgEMQLPIIALTAHalADEKQKL--LKVGMNDY 772
Cdd:cd19936   31 GASALDGLNAR------PPDLAILDIKMPRMDGMELLQRLRQ-------KSTLPVIFLTSK--DDEIDEVfgLRMGADDY 95

                 ....
gi 951237553 773 VTKP 776
Cdd:cd19936   96 ITKP 99
PRK11697 PRK11697
two-component system response regulator BtsR;
663-800 1.14e-05

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 47.53  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLP---NLIVLEALLGELNVkttkalSGQ-----EALNIIQeridqKLKPfDLVFMDIQMPVMSGIDttrai 734
Cdd:PRK11697   2 IKVLIVDDEPLareELRELLQEEGDIEI------VGEcsnaiEAIGAIH-----RLKP-DVVFLDIQMPRISGLE----- 64
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553 735 rsLESTLDGEmQLP-IIALTAH---AL-ADEKQKLlkvgmnDYVTKPIQMEQIIQILtQWTKNNFTAQNLA 800
Cdd:PRK11697  65 --LVGMLDPE-HMPyIVFVTAFdeyAIkAFEEHAF------DYLLKPIDPARLAKTL-ARLRQERSPQDVL 125
PLN03029 PLN03029
type-a response regulator protein; Provisional
663-782 1.42e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 47.34  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERIDQKLKP--------------FDLVFMDIQMPVMSGI 728
Cdd:PLN03029   9 FHVLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEDDRSNPdtpsvspnshqeveVNLIITDYCMPGMTGY 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 951237553 729 DTTRAIRSLESTLDgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:PLN03029  89 DLLKKIKESSSLRN----IPVVIMSSENVPSRITRCLEEGAEEFFLKPVQLSDL 138
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
716-788 1.47e-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: 44.89  E-value: 1.47e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951237553 716 VFMDIQMPVMSGIDTTRAIRSLEStldgemQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd17537   48 LVLDVRMPGMSGLELQDELLARGS------NIPIIFITGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
375-502 3.71e-05

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: 44.55  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 375 DMLSPLAAQKHIAMAFYYADNIpqQVIGDALRFKQILTNLISNAIKFTpDGEIIVRVRMEHDDigqclLHFSVQDSGIGL 454
Cdd:cd16954    8 SALNKVYQRKGVSISLDISPEL--RFPGERNDLMELLGNLLDNACKWC-LEFVEVTARQTDGG-----LHLIVDDDGPGV 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 951237553 455 SGTDRKKLFESFSQGDASVTrqfgGTGLGLAISKQLVHLMHGQIGFED 502
Cdd:cd16954   80 PESQRSKIFQRGQRLDEQRP----GQGLGLAIAKEIVEQYGGELSLSD 123
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
665-788 6.24e-05

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


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 43.63  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDhlpNLIVLEAL-----LGELNVKTtkALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLES 739
Cdd:cd17549    1 VLLVDD---DADVREALqqtleLAGFRVRA--FADAEEALAALSP------DFPGVVISDIRMPGMDGLELLAQIRELDP 69
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 951237553 740 tldgemQLPIIALTAH---ALADEKqklLKVGMNDYVTKPIQMEQIIQILTQ 788
Cdd:cd17549   70 ------DLPVILITGHgdvPMAVEA---MRAGAYDFLEKPFDPERLLDVVRR 112
PRK10816 PRK10816
two-component system response regulator PhoP;
714-783 7.15e-05

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 45.11  E-value: 7.15e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 714 DLVFMDIQMPVMSGIDTTRAIRSlestldGEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:PRK10816  46 DIAIVDLGLPDEDGLSLIRRWRS------NDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVM 109
PRK15115 PRK15115
response regulator GlrR; Provisional
664-777 9.33e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 45.98  E-value: 9.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHlPNLIVLEAL-LGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLd 742
Cdd:PRK15115   7 HLLLVDDD-PGLLKLLGMrLTSEGYSVVTAESGQEALRVLNR------EKVDLVISDLRMDEMDGMQLFAEIQKVQPGM- 78
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 951237553 743 gemqlPIIALTAHALADEKQKLLKVGMNDYVTKPI 777
Cdd:PRK15115  79 -----PVIILTAHGSIPDAVAATQQGVFSFLTKPV 108
PRK11517 PRK11517
DNA-binding response regulator HprR;
713-783 9.49e-05

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 44.89  E-value: 9.49e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553 713 FDLVFMDIQMPVMSGIDTTRAIRSLESTldgemqlPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:PRK11517  45 YALIILDIMLPGMDGWQILQTLRTAKQT-------PVICLTARDSVDDRVRGLDSGANDYLVKPFSFSELL 108
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
692-776 9.69e-05

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 42.60  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 692 ALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRSLEstldGEMQLPIIALTAHALADEKQKLLKVGMND 771
Cdd:cd17561   33 AHNGQEALELIEEK-----EP-DVLLLDIIMPHLDGIGVLEKLRRMR----LEKRPKIIMLTAFGQEDITQRAVELGASY 102

                 ....*
gi 951237553 772 YVTKP 776
Cdd:cd17561  103 YILKP 107
PRK15369 PRK15369
two component system response regulator;
665-775 1.07e-04

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 44.30  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHlpnlivleallgELNVKTTK-ALSGQEALNIIQERID--------QKLKPfDLVFMDIQMPVMSGIDTTRAIR 735
Cdd:PRK15369   6 ILLVDDH------------ELIINGIKnMLAPYPRYKIVGQVDNglevynacRQLEP-DIVILDLGLPGMNGLDVIPQLH 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 736 SLEStldgemQLPIIALTAHALADEKQKLLKVGMNDYVTK 775
Cdd:PRK15369  73 QRWP------AMNILVLTARQEEHMASRTLAAGALGYVLK 106
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-496 1.14e-04

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: 42.06  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 409 QILTNLISNA---IKFTPDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFESFSqgdasVTRQFG-GTGLGL 484
Cdd:cd16976    3 QVLMNLLQNAldaMGKVENPRIRIAARRLGGR-----LVLVVRDNGPGIAEEHLSRVFDPFF-----TTKPVGkGTGLGL 72
                         90
                 ....*....|..
gi 951237553 485 AISKQLVHlMHG 496
Cdd:cd16976   73 SISYGIVE-EHG 83
PRK10430 PRK10430
two-component system response regulator DcuR;
663-809 1.17e-04

two-component system response regulator DcuR;


Pssm-ID: 182454 [Multi-domain]  Cd Length: 239  Bit Score: 44.71  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 663 LHILAVDDhlpnlivlEALLGELNVKTTKALSG------QEALNIIQERIDQKLKPFDLVFMDIQMPVMSGIDTTRAIRS 736
Cdd:PRK10430   2 INVLIVDD--------DAMVAELNRRYVAQIPGfqccgtASTLEQAKEIIFNSDTPIDLILLDIYMQQENGLDLLPVLHE 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 951237553 737 LESTLDgemqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQIIQILTQWTKNnftaQNLAKDHHVVAEA 809
Cdd:PRK10430  74 AGCKSD------VIVISSAADAATIKDSLHYGVVDYLIKPFQASRFEEALTGWRQK----KMALEKHQYYDQA 136
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
678-775 1.41e-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: 42.26  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 678 LEALL---GELNVkTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRslestlDGEMQLPIIALTA 754
Cdd:cd19930   14 LAALLeleDDLEV-VAQASNGQEALRLVLK-----HSP-DVAILDIEMPGRTGLEVAAELR------EELPDTKVLIVTT 80
                         90       100
                 ....*....|....*....|.
gi 951237553 755 HALADEKQKLLKVGMNDYVTK 775
Cdd:cd19930   81 FGRPGYFRRALAAGVDGYVLK 101
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
713-783 1.58e-04

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 44.14  E-value: 1.58e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951237553 713 FDLVFMDIQMPVMSGIDTTRAIRSlestldGEMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:PRK09836  45 YDLIILDIMLPDVNGWDIVRMLRS------ANKGMPILLLTALGTIEHRVKGLELGADDYLVKPFAFAELL 109
glnL PRK11073
nitrogen regulation protein NR(II);
403-501 2.15e-04

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 44.69  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 403 DALRFKQILTNLISNAIKF--TPDGEIIVRVRMEHddigQCLLH---------FSVQDSGIGLSGTDRKKLFESFsqgda 471
Cdd:PRK11073 234 DPDQIEQVLLNIVRNALQAlgPEGGTITLRTRTAF----QLTLHgeryrlaarIDIEDNGPGIPPHLQDTLFYPM----- 304
                         90       100       110
                 ....*....|....*....|....*....|
gi 951237553 472 sVTRQFGGTGLGLAISKQLVHLMHGQIGFE 501
Cdd:PRK11073 305 -VSGREGGTGLGLSIARNLIDQHSGKIEFT 333
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
665-783 2.18e-04

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 43.94  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklkPF-DLVFMDIQMPVMSGIDTTRAIRSLESTLDg 743
Cdd:PRK10161   5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNE-------PWpDLILLDWMLPGGSGIQFIKHLKRESMTRD- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 951237553 744 emqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:PRK10161  77 ---IPVVMLTARGEEEDRVRGLETGADDYITKPFSPKELV 113
PRK15479 PRK15479
transcriptional regulator TctD;
715-782 2.99e-04

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 43.17  E-value: 2.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553 715 LVFMDIQMPVMSGIDTTRAIRSLESTLdgemqlPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQI 782
Cdd:PRK15479  47 LAVLDINMPGMDGLEVLQRLRKRGQTL------PVLLLTARSAVADRVKGLNVGADDYLPKPFELEEL 108
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
407-517 3.03e-04

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 41.21  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 407 FKQILTNLISNAIKFTPD-GEIIVRVRMEHDDIGQCLLH----------FSVQDSGIGLSGTDRKKLFESFsqgdaSVTR 475
Cdd:cd16919    1 LELAILNLAVNARDAMPEgGRLTIETSNQRVDADYALNYrdlipgnyvcLEVSDTGSGMPAEVLRRAFEPF-----FTTK 75
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 951237553 476 QFG-GTGLGLAISKQLVHLMHGQIGFEdnqerAPTDKGSTF--WF 517
Cdd:cd16919   76 EVGkGTGLGLSMVYGFVKQSGGHLRIY-----SEPGVGTTVriYL 115
ompR PRK09468
osmolarity response regulator; Provisional
661-776 3.28e-04

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 43.42  E-value: 3.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 661 QGLHILAVDDHLPNLIVLEALLGELNVkTTKALSGQEALNIIQERidqklKPFDLVFMDIQMPVMSGIDTTRAIRSLESt 740
Cdd:PRK09468   4 ENYKILVVDDDMRLRALLERYLTEQGF-QVRSAANAEQMDRLLTR-----ESFHLMVLDLMLPGEDGLSICRRLRSQNN- 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 951237553 741 ldgemQLPIIALTAHAlaDEKQKL--LKVGMNDYVTKP 776
Cdd:PRK09468  77 -----PTPIIMLTAKG--EEVDRIvgLEIGADDYLPKP 107
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
700-780 3.95e-04

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: 40.73  E-value: 3.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 700 NIIQERIDqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLestldgeMQLPIIALTAHALADEKQKLLKVGMNDYVTKPIQM 779
Cdd:cd18159   33 DVLEEFLQ--FKP-DLVLLDINLPYFDGFYWCREIRQI-------SNVPIIFISSRDDNMDQVMAINMGGDDYITKPFDL 102

                 .
gi 951237553 780 E 780
Cdd:cd18159  103 D 103
PRK10336 PRK10336
two-component system response regulator QseB;
690-782 4.04e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 42.96  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 690 TKALSGQEALniiqeridqKLKPFDLVFMDIQMPVMSGIDTTRAIRslestlDGEMQLPIIALTAHALADEKQKLLKVGM 769
Cdd:PRK10336  31 TQGRQGKEAL---------YSAPYDAVILDLTLPGMDGRDILREWR------EKGQREPVLILTARDALAERVEGLRLGA 95
                         90
                 ....*....|...
gi 951237553 770 NDYVTKPIQMEQI 782
Cdd:PRK10336  96 DDYLCKPFALIEV 108
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
664-790 4.70e-04

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: 41.83  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRSLEStldg 743
Cdd:COG4567    6 SLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQA------PPDYAVLDLRLGDGSGLDLIEALRERDP---- 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 951237553 744 emQLPIIALTAH---ALADEKQKLlkvGMNDYVTKPIQMEQIIQILTQWT 790
Cdd:COG4567   76 --DARIVVLTGYasiATAVEAIKL---GADDYLAKPADADDLLAALERAE 120
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
665-777 8.13e-04

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 40.05  E-value: 8.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDD--HLPNLIVleALLGELNVKTTKALSGQEALNIIQERidqklKPfDLVFMDIQMPVMSGIDTTRAIRslestld 742
Cdd:cd17622    3 ILLVEDdpKLARLIA--DFLESHGFNVVVEHRGDRALEVIARE-----KP-DAVLLDIMLPGIDGLTLCRDLR------- 67
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 951237553 743 GEMQLPIIALTAHAlADEKQKL-LKVGMNDYVTKPI 777
Cdd:cd17622   68 PKYQGPILLLTALD-SDIDHILgLELGADDYVVKPV 102
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
665-776 9.44e-04

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


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 39.69  E-value: 9.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqKLKPFDLVFMDIQMPVMSGIDTTRAIRSLESTLDge 744
Cdd:cd17582    1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLED----EQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKN-- 74
                         90       100       110
                 ....*....|....*....|....*....|..
gi 951237553 745 mqLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:cd17582   75 --IPVIMMSSQDSVGVVFKCLSKGAADYLVKP 104
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
87-496 1.28e-03

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 42.31  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553  87 IMQSMFSEKNLKRAALIDSNGQTYLSIGYRDNRYWPNFTQNNNFFGPISYNHNNIYGVRIIDTAGKPPVW-LLIEMDNQP 165
Cdd:COG2972   68 LLLLLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALILLLALLLLLSILLLILGLLLIILLLLSLLGWtLVSLIPKSE 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 166 LELARYRILIALVITGLMTLLLLLLCLNFYSRRWIAPMYEIRMQLQRLNADTLdQHIVINSSGELRLLQRDIANVVKRLH 245
Cdd:COG2972  148 LFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDL-VRLEVSGNDEIGILARSFNEMVERIK 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 246 fsflELKEHTEQTEEDLRrtldtlevqnityrQARDQAISSnQAKSVFLANIshelrtpLNSIDGFIHL----------- 314
Cdd:COG2972  227 ----ELIEEVYELELEKK--------------EAELKALQA-QINPHFLFNT-------LNSIRWLAELedpeeaeemle 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 315 ----LLRQqNLSNEQNLylQTIRKSsahlLALINDVLDFSKIDAG-KLELEtapFDLEEavfDVMDMLSPlaaqkhiama 389
Cdd:COG2972  281 alskLLRY-SLSKGDEL--VTLEEE----LELIKSYLEIQKLRFGdRLEVE---IEIDE---ELLDLLIP---------- 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 390 fyyadnipqqvigdalrfKQILTNLISNAIKF-----TPDGEIIVRVRMEHDDIgqcllHFSVQDSGIGLSGTDRKKLFE 464
Cdd:COG2972  338 ------------------KLILQPLVENAIEHgiepkEGGGTIRISIRKEGDRL-----VITVEDNGVGMPEEKLEKLLE 394
                        410       420       430
                 ....*....|....*....|....*....|..
gi 951237553 465 SFSQGDasvtrqfGGTGLGLAISKQLVHLMHG 496
Cdd:COG2972  395 ELSSKG-------EGRGIGLRNVRERLKLYYG 419
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
665-776 1.32e-03

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 41.59  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 665 ILAVDDhlpnlivlEALLGEL--------NVKTTKALSGQEALNIIQERidqklkPFDLVFMDIQMPVMSGIDTTRAIRS 736
Cdd:PRK10710  13 ILIVED--------EPKLGQLlidylqaaSYATTLLSHGDEVLPYVRQT------PPDLILLDLMLPGTDGLTLCREIRR 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 951237553 737 LEstldgemQLPIIALTAHalADEKQKL--LKVGMNDYVTKP 776
Cdd:PRK10710  79 FS-------DIPIVMVTAK--IEEIDRLlgLEIGADDYICKP 111
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
410-501 1.49e-03

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 42.21  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 410 ILTNLISN---AIKFTPDGEIIVRVRMEHDDigqclLHFSVQDSGIGLSGTDRKKLFES-FS-QGDasvtrqfgGTGLGL 484
Cdd:PRK11086 437 ILGNLIENaleAVGGEEGGEISVSLHYRNGW-----LHCEVSDDGPGIAPDEIDAIFDKgYStKGS--------NRGVGL 503
                         90
                 ....*....|....*..
gi 951237553 485 AISKQLVHLMHGQIGFE 501
Cdd:PRK11086 504 YLVKQSVENLGGSIAVE 520
fixJ PRK09390
response regulator FixJ; Provisional
712-783 1.53e-03

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 40.76  E-value: 1.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 951237553 712 PFDLVFMDIQMPVMSGIDTTRAIRSLESTldgemqLPIIALTAHA---LADEKQKLlkvGMNDYVTKPIQMEQII 783
Cdd:PRK09390  47 RFGCVVTDVRMPGIDGIELLRRLKARGSP------LPVIVMTGHGdvpLAVEAMKL---GAVDFIEKPFEDERLI 112
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
716-783 1.68e-03

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: 40.47  E-value: 1.68e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 951237553 716 VFMDIQMPVMSGIDTTRAIRSLESTldgemqLPIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQII 783
Cdd:COG4566   47 LLLDVRMPGMSGLELQEELAARGSP------LPVIFLTGHGDVPMAVRAMKAGAVDFLEKPFDDQALL 108
pleD PRK09581
response regulator PleD; Reviewed
659-788 2.01e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 41.81  E-value: 2.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 659 NGQGLHILAVDDhlpNLIVLEALLGELNVKT--TKALSGQEALNIIQERidqklkPFDLVFMDIQMpvmSGIDTTR---A 733
Cdd:PRK09581 152 KDEDGRILLVDD---DVSQAERIANILKEEFrvVVVSDPSEALFNAAET------NYDLVIVSANF---ENYDPLRlcsQ 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 951237553 734 IRSLESTldgeMQLPIIALTAhalADEKQKLLK---VGMNDYVTKPI-QMEQIIQILTQ 788
Cdd:PRK09581 220 LRSKERT----RYVPILLLVD---EDDDPRLVKaleLGVNDYLMRPIdKNELLARVRTQ 271
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
711-776 2.89e-03

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 40.17  E-value: 2.89e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 951237553 711 KPfDLVFMDIQMPVMSGIDTTRAIRSLEStldgemqLPIIALTAHALADEKQKLLKVGMNDYVTKP 776
Cdd:PRK10529  45 KP-DLIILDLGLPDGDGIEFIRDLRQWSA-------IPVIVLSARSEESDKIAALDAGADDYLSKP 102
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
690-777 5.27e-03

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


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 38.06  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 690 TKALSGQEALnIIQERIDQKL-----KPFDLVFMDIQMPVMSGIDTTRAIRSLESTldgeMQLPIIALtahALADEKQKL 764
Cdd:cd17539   15 AAMLSSEHEV-VVEADPDEALfraaeGPFDLVIVSLALEDFDGLRLCSQLRSLERT----RQLPILAV---ADPGDRGRL 86
                         90
                 ....*....|....*.
gi 951237553 765 LK---VGMNDYVTKPI 777
Cdd:cd17539   87 IRaleIGVNDYLVRPI 102
PRK10693 PRK10693
two-component system response regulator RssB;
692-777 5.47e-03

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 39.97  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 692 ALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRslestLDGeMQLPIIALTAHALADEKQKLLKVGMND 771
Cdd:PRK10693   3 AANGVDALELLGG-----FTP-DLIICDLAMPRMNGIEFVEHLR-----NRG-DQTPVLVISATENMADIAKALRLGVQD 70

                 ....*.
gi 951237553 772 YVTKPI 777
Cdd:PRK10693  71 VLLKPV 76
PRK10766 PRK10766
two-component system response regulator TorR;
664-837 5.67e-03

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 39.25  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 664 HILAVDDHLPNLIVLEALLGELNVKTTKALSGQEALNIIQEridqklKPFDLVFMDIQMPVMSGIDTTRAIRSlESTLDg 743
Cdd:PRK10766   4 HILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQN------QHVDLILLDINLPGEDGLMLTRELRS-RSTVG- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 744 emqlpIIALTAHALADEKQKLLKVGMNDYVTKPIQMEQiiqiLTQWTKNNFTAQNLAKDHHVVAEALDPEILNWQQSLQL 823
Cdd:PRK10766  76 -----IILVTGRTDSIDRIVGLEMGADDYVTKPLELRE----LLVRVKNLLWRISLARQAQPHAQEEDNCYRFAGYCLNV 146
                        170
                 ....*....|....
gi 951237553 824 AANKEDLAQDLLKM 837
Cdd:PRK10766 147 SRRTLERNGEPIKL 160
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
684-777 6.46e-03

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 37.25  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951237553 684 ELNVKTTKALSGQEALNIIQEridqkLKPfDLVFMDIQMPVMSGIDTTRAIRSLEStldgemQLPIIALTAHALADEKQK 763
Cdd:cd17565   22 DLGEVVGEADNGAQAYDEILF-----LQP-DIVLIDLLMPGMDGIQLVRKLKDTGS------NGKFIMISQVSDKEMIGK 89
                         90
                 ....*....|....
gi 951237553 764 LLKVGMNDYVTKPI 777
Cdd:cd17565   90 AYQAGIEFFINKPI 103
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
665-734 7.70e-03

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 39.48  E-value: 7.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 951237553 665 ILAVDDhLPnlIVLEALlgelnvktTKALSGQEALNII------QERIDQ-KLKPFDLVFMDIQMPVMSGIDTTRAI 734
Cdd:PRK12555   3 IGIVND-SP--LAVEAL--------RRALARDPDHEVVwvatdgAQAVERcAAQPPDVILMDLEMPRMDGVEATRRI 68
 
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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