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Conserved domains on  [gi|1237881481|gb|PAJ75310|]
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hypothetical protein CJF42_05990 [Pseudoalteromonas sp. NBT06-2]

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
320-954 4.71e-100

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: 336.82  E-value: 4.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  320 LAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLT 399
Cdd:PRK11107   281 LAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLV 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  400 LETSKFklyDLFENLSENLSIF---AYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVS 476
Cdd:PRK11107   361 LENIPF---SLRETLDEVVTLLahsAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRA 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQ 556
Cdd:PRK11107   438 LSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  557 LKIVPNEPSLQPYINKFKNINTLVINESMAVKNIITQMLREFGMMVTSAEsgydalSIFSSEQASRPFELILMdwkmsSD 636
Cdd:PRK11107   518 LDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSP------TLSQLPEAHYDILLLGL-----PV 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  637 NDFKVLEKIHYLVTTNNYMRPKIILVTD-YGQEEFDLVTNDlGVDAFVNKPVTPYNMAKSLLiafneslnDITHHLPETN 715
Cdd:PRK11107   587 TFREPLTMLHERLAKAKSMTDFLILALPcHEQVLAEQLKQD-GADACLSKPLSHTRLLPALL--------EPCHHKQPPL 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  716 NLNNMTKLLAgSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKE 795
Cdd:PRK11107   658 LPPTDESRLP-LTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQL 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  796 LNLSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEIFTSLSEQENInlSHNSN-IINFQV 874
Cdd:PRK11107   737 PHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEP--VHFPNaTLDWQL 814
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  875 GLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQETDD 954
Cdd:PRK11107   815 ALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSVED 894
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
320-954 4.71e-100

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 336.82  E-value: 4.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  320 LAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLT 399
Cdd:PRK11107   281 LAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLV 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  400 LETSKFklyDLFENLSENLSIF---AYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVS 476
Cdd:PRK11107   361 LENIPF---SLRETLDEVVTLLahsAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRA 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQ 556
Cdd:PRK11107   438 LSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  557 LKIVPNEPSLQPYINKFKNINTLVINESMAVKNIITQMLREFGMMVTSAEsgydalSIFSSEQASRPFELILMdwkmsSD 636
Cdd:PRK11107   518 LDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSP------TLSQLPEAHYDILLLGL-----PV 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  637 NDFKVLEKIHYLVTTNNYMRPKIILVTD-YGQEEFDLVTNDlGVDAFVNKPVTPYNMAKSLLiafneslnDITHHLPETN 715
Cdd:PRK11107   587 TFREPLTMLHERLAKAKSMTDFLILALPcHEQVLAEQLKQD-GADACLSKPLSHTRLLPALL--------EPCHHKQPPL 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  716 NLNNMTKLLAgSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKE 795
Cdd:PRK11107   658 LPPTDESRLP-LTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQL 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  796 LNLSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEIFTSLSEQENInlSHNSN-IINFQV 874
Cdd:PRK11107   737 PHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEP--VHFPNaTLDWQL 814
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  875 GLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQETDD 954
Cdd:PRK11107   815 ALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSVED 894
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
319-962 4.84e-71

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 256.24  E-value: 4.84e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  319 RLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKL 398
Cdd:TIGR02956  451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  399 TLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVmevsRK 478
Cdd:TIGR02956  531 SISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV----SL 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  479 DTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNittqlk 558
Cdd:TIGR02956  607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFW------ 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  559 ivpnepslqpyinkfknintlvinesmavkniitqmlrefgmmvtsaesgydalsifsseqasrpFELILMDWKMSSDND 638
Cdd:TIGR02956  679 -----------------------------------------------------------------FTLPLTRGKPAEDSA 693
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  639 FKVLEKIHylvttnnymrpkiilvtdygqeefdlvtndlgvdafvnkpvtpynmakslliafneslndithhlpetnnln 718
Cdd:TIGR02956  694 TLTVIDLP------------------------------------------------------------------------ 701
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  719 nmtkllaGSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRK-ELN 797
Cdd:TIGR02956  702 -------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAiYGA 774
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  798 LSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSK-----PEIFTSLS----------EQENIN 862
Cdd:TIGR02956  775 KNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKsnteaPVLSASPSfdsasvienaQADDIP 854
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  863 LSHNSNIINF---QVGLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLA 939
Cdd:TIGR02956  855 ESNQASEFLLdeeQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLC 934
                          650       660
                   ....*....|....*....|....*
gi 1237881481  940 EQLERSFDDGQET--DDNLIKQVKL 962
Cdd:TIGR02956  935 QQLEKQGKTGALElsDIDEIKQAWQ 959
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
264-554 9.46e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 236.34  E-value: 9.46e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  264 LLYNFHGTQLLLYKNRFNLNPLLPLLSSIFIISLLILIYIIQKSTSSIVSMSSRMRLAKIQAEKANETKTHFLNNISHEI 343
Cdd:COG0642     42 LLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHEL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  344 RTPMNAIIGLSHILINsDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSKFKLYDLFENLSENLSIFAY 423
Cdd:COG0642    122 RTPLTAIRGYLELLLE-ELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAE 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  424 DKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFTEYGEVIvTVmEVSRKDTDIILKfnIKDSGAGINLKDIEHV 503
Cdd:COG0642    201 EKGIELELDLPDDLPTVR-GDPDRLRQVLLNLLSNAIKYTPEGGTV-TV-SVRREGDRVRIS--VEDTGPGIPPEDLERI 275
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  504 FDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG0642    276 FEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
448-557 5.28e-49

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: 169.21  E-value: 5.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAI 527
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  528 SQKFIELMGGEIWVESEVGKGSEFNITTQL 557
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
443-554 1.08e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 119.68  E-value: 1.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481   443 GDQTKLNQVLLNIVNNAIKFT-EYGEVIVTVmevsrKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSlTRKHGGT 521
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTL-----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1237881481   522 GLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTIT 107
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
443-559 2.70e-27

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: 107.07  E-value: 2.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  443 GDQTKLNQVLLNIVNNAIKFTEY-GEVIVTVmevsrkDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADgslTRKHGGT 521
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITVTL------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1237881481  522 GLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLKI 559
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
335-554 9.91e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.18  E-value: 9.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPmnaiigLSHILINSDLNKKQRQHLD-KVHKSAEsLL--------SIINNILDFSNIEADKLTLETSKF 405
Cdd:NF040691   274 FVSDVSHELRTP------LTTIRMAADVIHDSRDDFDpATARSAE-LLhteldrfeSLLSDLLEISRFDAGAAELDVEPV 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  406 KLYDLFENLSENLSIFAYDKNIELIFDIPvALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTvmeVSRKDTDIILK 485
Cdd:NF040691   347 DLRPLVRRVVDALRQLAERAGVELRVDAP-GTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT---VAQDDTAVAVT 422
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237881481  486 fnIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:NF040691   423 --VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
319-539 8.30e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 93.74  E-value: 8.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  319 RLAKIqAEKANETKTHFLNNISHEIRTPMnAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKL 398
Cdd:NF012163   228 QLAST-LEKNEQMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGAL 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  399 TLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALedIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRK 478
Cdd:NF012163   306 AYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGGSL----HISAS 379
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  479 DTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEI 539
Cdd:NF012163   380 QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
resp_reg_YycF NF040534
response regulator YycF;
729-836 2.18e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 55.88  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELnlsELPIIAMIA 808
Cdd:NF040534     3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY---DMPIIMLTA 79
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:NF040534    80 KDSEIDKVLGLELGADDYVTKPFSTREL 107
 
Name Accession Description Interval E-value
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
320-954 4.71e-100

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 336.82  E-value: 4.71e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  320 LAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLT 399
Cdd:PRK11107   281 LAKKRAQEAARIKSEFLANMSHELRTPLNGVIGFTRQTLKTPLTPTQRDYLQTIERSANNLLAIINDILDFSKLEAGKLV 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  400 LETSKFklyDLFENLSENLSIF---AYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVS 476
Cdd:PRK11107   361 LENIPF---SLRETLDEVVTLLahsAHEKGLELTLNIDPDVPDNVIGDPLRLQQIITNLVGNAIKFTESGNIDILVELRA 437
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQ 556
Cdd:PRK11107   438 LSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQADASISRRHGGTGLGLVITQKLVNEMGGDISFHSQPNRGSTFWFHLP 517
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  557 LKIVPNEPSLQPYINKFKNINTLVINESMAVKNIITQMLREFGMMVTSAEsgydalSIFSSEQASRPFELILMdwkmsSD 636
Cdd:PRK11107   518 LDLNPNPIIDGLPTDCLAGKRLLYVEPNSAAAQATLDILSETPLEVTYSP------TLSQLPEAHYDILLLGL-----PV 586
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  637 NDFKVLEKIHYLVTTNNYMRPKIILVTD-YGQEEFDLVTNDlGVDAFVNKPVTPYNMAKSLLiafneslnDITHHLPETN 715
Cdd:PRK11107   587 TFREPLTMLHERLAKAKSMTDFLILALPcHEQVLAEQLKQD-GADACLSKPLSHTRLLPALL--------EPCHHKQPPL 657
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  716 NLNNMTKLLAgSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKE 795
Cdd:PRK11107   658 LPPTDESRLP-LTVMAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQL 736
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  796 LNLSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEIFTSLSEQENInlSHNSN-IINFQV 874
Cdd:PRK11107   737 PHNQNTPIIAVTAHAMAGERERLLSAGMDDYLAKPIDEAMLKQVLLRYKPGPKFTSRVVAPEPPEP--VHFPNaTLDWQL 814
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  875 GLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQETDD 954
Cdd:PRK11107   815 ALRQAAGKPDLARDMLQMLLDFLPEVRNKVEEALAGEDPEGLLDLIHKLHGSCSYSGVPRLKKLCQLIEQQLRSGTSVED 894
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
319-962 4.84e-71

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


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 256.24  E-value: 4.84e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  319 RLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKL 398
Cdd:TIGR02956  451 AKARAEAEEANRAKSAFLATMSHEIRTPLNGILGTLELLGDTGLTSQQQQYLQVINRSGESLLDILNDILDYSKIEAGHL 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  399 TLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVmevsRK 478
Cdd:TIGR02956  531 SISPRPFDLNALLDDVHHLMVSRAQLKGIQLRLNIPEQLPNWWQGDGPRIRQVLINLVGNAIKFTDRGSVVLRV----SL 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  479 DTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNittqlk 558
Cdd:TIGR02956  607 NDDSSLLFEVEDTGCGIAEEEQATLFDAFTQADGR--RRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFW------ 678
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  559 ivpnepslqpyinkfknintlvinesmavkniitqmlrefgmmvtsaesgydalsifsseqasrpFELILMDWKMSSDND 638
Cdd:TIGR02956  679 -----------------------------------------------------------------FTLPLTRGKPAEDSA 693
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  639 FKVLEKIHylvttnnymrpkiilvtdygqeefdlvtndlgvdafvnkpvtpynmakslliafneslndithhlpetnnln 718
Cdd:TIGR02956  694 TLTVIDLP------------------------------------------------------------------------ 701
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  719 nmtkllaGSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRK-ELN 797
Cdd:TIGR02956  702 -------PQRVLLVEDNEVNQMVAQGFLTRLGHKVTLAESGQSALECFHQHAFDLALLDINLPDGDGVTLLQQLRAiYGA 774
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  798 LSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSK-----PEIFTSLS----------EQENIN 862
Cdd:TIGR02956  775 KNEVKFIAFSAHVFNEDVAQYLAAGFDGFLAKPVVEEQLTAMIAVILAGGKsnteaPVLSASPSfdsasvienaQADDIP 854
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  863 LSHNSNIINF---QVGLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLA 939
Cdd:TIGR02956  855 ESNQASEFLLdeeQLQQDIEVLGVEKVRQLVALFKTSSAEQLEELSAARAVDDDAQIKKLAHKLKGSAGSLGLTQLTQLC 934
                          650       660
                   ....*....|....*....|....*
gi 1237881481  940 EQLERSFDDGQET--DDNLIKQVKL 962
Cdd:TIGR02956  935 QQLEKQGKTGALElsDIDEIKQAWQ 959
PRK15347 PRK15347
two component system sensor kinase;
321-969 1.39e-70

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 254.18  E-value: 1.39e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  321 AKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTL 400
Cdd:PRK15347   387 AKQRAEQANKRKSEHLTTISHEIRTPLNGVLGALELLQNTPLTAEQMDLADTARQCTLSLLAIINNLLDFSRIESGQMTL 466
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  401 ETSKFKLYDLFENLSENLSIFAYDKNIEL-IF---DIPVALEDiyigDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMevS 476
Cdd:PRK15347   467 SLEETALLPLLDQAMLTIQGPAQSKSLTLrTFvgaHVPLYLHL----DSLRLRQILVNLLGNAVKFTETGGIRLRVK--R 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTdiiLKFNIKDSGAGINLKDIEHVFDAFCQADGSLtrkhGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQ 556
Cdd:PRK15347   541 HEQQ---LCFTVEDTGCGIDIQQQQQIFTPFYQADTHS----QGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLP 613
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  557 LkIVPNEPslqpyinkfknintLVINESMAVKNIITQMLREFGMmvtSAESGYDALSIFSSEQASRPFELilmdwkmssd 636
Cdd:PRK15347   614 L-NEYAPP--------------EPLKGELSAPLALHRQLSAWGI---TCQPGHQNPALLDPELAYLPGRL---------- 665
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  637 ndfkvlekihylvttnnYMRPKIILvtdYGQEEfdlvtndlgvDAFVNKPVTPYNMakslliafneslndithhlpetnn 716
Cdd:PRK15347   666 -----------------YDLLQQII---QGAPN----------EPVINLPLQPWQL------------------------ 691
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  717 lnnmtkllagsNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKEL 796
Cdd:PRK15347   692 -----------QILLVDDVETNRDIIGMMLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDP 760
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  797 NL--SELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMrkwitpskpEIFTSLSEQENINLSHNSniinfqv 874
Cdd:PRK15347   761 NNldPDCMIVALTANAAPEEIHRCKKAGMNHYLTKPVTLAQLARAL---------ELAAEYQLLRGIELSPQD------- 824
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  875 glEICSGSVSLYQ-KLLKKFADSECDFLQRFENLIleKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQETD 953
Cdd:PRK15347   825 --SSCSPLLDTDDmALNSKLYQSLLLLLAQIEQAV--ENQEVLSQLLHTLKGCAGQAGLTELQCAVIDLENALETGEILS 900
                          650
                   ....*....|....*.
gi 1237881481  954 DNLIKQVKLIDEKIFE 969
Cdd:PRK15347   901 LEELTDLRELIHALFK 916
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
264-554 9.46e-70

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 236.34  E-value: 9.46e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  264 LLYNFHGTQLLLYKNRFNLNPLLPLLSSIFIISLLILIYIIQKSTSSIVSMSSRMRLAKIQAEKANETKTHFLNNISHEI 343
Cdd:COG0642     42 LLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLLLEEANEAKSRFLANVSHEL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  344 RTPMNAIIGLSHILINsDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSKFKLYDLFENLSENLSIFAY 423
Cdd:COG0642    122 RTPLTAIRGYLELLLE-ELDEEQREYLETILRSADRLLRLINDLLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAE 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  424 DKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFTEYGEVIvTVmEVSRKDTDIILKfnIKDSGAGINLKDIEHV 503
Cdd:COG0642    201 EKGIELELDLPDDLPTVR-GDPDRLRQVLLNLLSNAIKYTPEGGTV-TV-SVRREGDRVRIS--VEDTGPGIPPEDLERI 275
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  504 FDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG0642    276 FEPFFRTDPS--RRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTVT 324
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
326-943 8.53e-68

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 243.31  E-value: 8.53e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  326 EKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSKF 405
Cdd:PRK11091   277 EKASRDKTTFISTISHELRTPLNGIVGLSRILLDTELTAEQRKYLKTIHVSAITLGNIFNDIIDMDKMERRKLQLDNQPI 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  406 KLYDLFENLsENLS-IFAYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVmevsRKDTDIIL 484
Cdd:PRK11091   357 DFTDFLADL-ENLSgLQAEQKGLRFDLEPLLPLPHKVITDGTRLRQILWNLISNAVKFTQQGGVTVRV----RYEEGDML 431
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  485 KFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHG-GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLKIVPNE 563
Cdd:PRK11091   432 TFEVEDSGIGIPEDELDKIFAMYYQVKDSHGGKPAtGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHAPAVAEE 511
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  564 PSLQPyinkfknintlvinesmavkniitqmlrefgmmvtsaesgydalsifsseqasrpfelilmdwkmssdndfkvle 643
Cdd:PRK11091   512 VEDAF--------------------------------------------------------------------------- 516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  644 kihylvTTNNYMRPKIilvtdygqeefdlvtndlgvdafvnkpvtpynmakslliafneslndithhlpetnnlnnmtkl 723
Cdd:PRK11091   517 ------DEDDMPLPAL---------------------------------------------------------------- 526
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  724 lagsNILLVEDNEINSEVTSSLL-SL-HKINVtcAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSEL 801
Cdd:PRK11091   527 ----NILLVEDIELNVIVARSVLeKLgNSVDV--AMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIARELRERYPREDL 600
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  802 -PIIAMIANtMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEiftSLSEQENINLSHNSNIINFQ------- 873
Cdd:PRK11091   601 pPLVALTAN-VLKDKKEYLDAGMDDVLSKPLSVPALTAMIKKFWDTQDDE---ESTVTTEESSKANEALLDIPmleqyve 676
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  874 -VGLEICSGSVSLYQKLLKkfadsecDFLQrfenlILEKNRSAAKR-----QAHSLRGVSGNIGAANINNLAEQLE 943
Cdd:PRK11091   677 lVGPKLITDSLAVFEKMMP-------GYLS-----VLDSNLTARDQkgiveEAHKIKGAAGSVGLRHLQQLAQQIQ 740
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
324-554 3.96e-63

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 219.81  E-value: 3.96e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  324 QAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINS--DLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLE 401
Cdd:COG5002    157 ELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGaaDDPEERREYLEIILEEAERLSRLVNDLLDLSRLESGELKLE 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  402 TSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFT-EYGEVIVTVmevSRKDT 480
Cdd:COG5002    237 KEPVDLAELLEEVVEELRPLAEEKGIELELDLPEDPLLVL-GDPDRLEQVLTNLLDNAIKYTpEGGTITVSL---REEDD 312
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  481 DIILKfnIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG5002    313 QVRIS--VRDTGIGIPEEDLPRIFERFYRVDKSRSRETGGTGLGLAIVKHIVEAHGGRIWVESEPGKGTTFTIT 384
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
317-554 5.58e-63

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


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 214.00  E-value: 5.58e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  317 RMRLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSD--LNKKQRQHLDKVHKSAESLLSIINNILDFSNIE 394
Cdd:COG2205      1 ELEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLDEEdlSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  395 ADKLTLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFTEYGEVIVtvME 474
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKGIRLELDLPPELPLVY-ADPELLEQVLANLLDNAIKYSPPGGTIT--IS 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  475 VSRKDTDIILKfnIKDSGAGINLKDIEHVFDAFCQADGslTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG2205    158 ARREGDGVRIS--VSDNGPGIPEEELERIFERFYRGDN--SRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVT 233
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
325-830 4.50e-51

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 195.19  E-value: 4.50e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  325 AEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSK 404
Cdd:PRK10841   440 AEQASQSKSMFLATVSHELRTPLYGIIGNLDLLQTKELPKGVDRLVTAMNNSSSLLLKIISDILDFSKIESEQLKIEPRE 519
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  405 FKLYDLFENLSEN---------LSIFAYdknIELifDIPVALEdiyiGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVmeV 475
Cdd:PRK10841   520 FSPREVINHITANylplvvkkrLGLYCF---IEP--DVPVALN----GDPMRLQQVISNLLSNAIKFTDTGCIVLHV--R 588
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  476 SRKDtdiILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI-- 553
Cdd:PRK10841   589 VDGD---YLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIri 665
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  554 ---TTQLKIVPNEPSLQPyinkfKNINTLVINESMAvkNIITQMLREFGMMVTSAEsgydalsifssEQASRPFELILmd 630
Cdd:PRK10841   666 plyGAQYPQKKGVEGLQG-----KRCWLAVRNASLE--QFLETLLQRSGIQVQRYE-----------GQEPTPEDVLI-- 725
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  631 wkmsSDNDFKVLEKIHYLVttnnymrpkiilvtdygqeEFDLVTNDLGVDAFVNKPVtpYNMAKSL-LIAFNESLNDITH 709
Cdd:PRK10841   726 ----TDDPVQKKWQGRAVI-------------------TFCRRHIGIPLEIAPGEWV--HSTATPHeLPALLARIYRIEL 780
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  710 HLPETNNLNNMTKLLAGSN----ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDG 785
Cdd:PRK10841   781 ESDDSANALPSTDKAVSDNddmmILVVDDHPINRRLLADQLGSLGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDG 860
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1237881481  786 YKATQVIRkELNLSeLPIIAMIANTMLADKNKALDCGMNDYIEKP 830
Cdd:PRK10841   861 YRLTQRLR-QLGLT-LPVIGVTANALAEEKQRCLEAGMDSCLSKP 903
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
448-557 5.28e-49

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: 169.21  E-value: 5.28e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAI 527
Cdd:cd16922      1 LRQILLNLLGNAIKFTEEGEVTLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSQADSSTTRKYGGTGLGLAI 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  528 SQKFIELMGGEIWVESEVGKGSEFNITTQL 557
Cdd:cd16922     81 SKKLVELMGGDISVESEPGQGSTFTFTLPL 110
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
319-633 4.13e-44

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 173.55  E-value: 4.13e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  319 RLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEA--D 396
Cdd:PRK11466   431 RQARAEAEKASQAKSAFLAAMSHEIRTPLYGILGTAQLLADNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAggK 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  397 KLTLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTvmevS 476
Cdd:PRK11466   511 NVSVSDEPFEPRPLLESTLQLMSGRVKGRPIRLATDIADDLPTALMGDPRRIRQVITNLLSNALRFTDEGSIVLR----S 586
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILkFNIKDSGAGINLKDIEHVFDAFCQADGsltrKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQ 556
Cdd:PRK11466   587 RTDGEQWL-VEVEDSGCGIDPAKLAEIFQPFVQVSG----KRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLP 661
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  557 LKIV---PNEPSLQPYinKFKNINTLVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseQASRPFELILMDWKM 633
Cdd:PRK11466   662 LRVAtapVPKTVNQAV--RLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETL---QNSEPFAAALVDFDL 736
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
317-554 1.02e-41

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


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 160.72  E-value: 1.02e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  317 RMRLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILI---NSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNI 393
Cdd:COG4251    267 ELEERTAELERSNEELEQFAYVASHDLREPLRKISGFSQLLEedyGDKLDEEGREYLERIRDAAERMQALIDDLLAYSRV 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  394 EADKLTLETskFKLYDLFENLSENLSIFAYDKNIELIFDipvALEDIYiGDQTKLNQVLLNIVNNAIKFTeyGEVIVTVM 473
Cdd:COG4251    347 GRQELEFEP--VDLNELLEEVLEDLEPRIEERGAEIEVG---PLPTVR-GDPTLLRQVFQNLISNAIKYS--RPGEPPRI 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  474 EVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:COG4251    419 EIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSR--DEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYF 496

                   .
gi 1237881481  554 T 554
Cdd:COG4251    497 T 497
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
729-840 3.46e-41

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: 146.85  E-value: 3.46e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRK-ELNLSELPIIAMI 807
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRElEGGGRRTPIIALT 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIM 840
Cdd:cd17546     81 ANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
724-849 1.69e-39

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: 142.68  E-value: 1.69e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  724 LAGSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPI 803
Cdd:COG0784      3 LGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIPI 82
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1237881481  804 IAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKP 849
Cdd:COG0784     83 IALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
339-554 1.53e-35

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: 142.04  E-value: 1.53e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHILiNSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKltleTSKFKLYDLFENLSENL 418
Cdd:COG5809    277 IAHEIRNPLTSLKGFIQLL-KDTIDEEQKTYLDIMLSELDRIESIISEFLVLAKPQAIK----YEPKDLNTLIEEVIPLL 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  419 SIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFT-EYGEVIVtvmEVSRKDTDIILkFNIKDSGAGINL 497
Cdd:COG5809    352 QPQALLKNVQIELELEDDIPDIL-GDENQLKQVFINLLKNAIEAMpEGGNITI---ETKAEDDDKVV-ISVTDEGCGIPE 426
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  498 KDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG5809    427 ERLKKLGEPF------YTTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKGTTFSIT 477
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
339-554 9.71e-35

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


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 136.85  E-value: 9.71e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHIL---INSDLNKKQ-RQHLDKVHKSAESLLSIINNILDFSnieaDKLTLETSKFKLYDLFENL 414
Cdd:COG4191    149 IAHEINNPLAAILGNAELLrrrLEDEPDPEElREALERILEGAERAAEIVRSLRAFS----RRDEEEREPVDLNELIDEA 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  415 SENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAI---KFTEYGEVIVTVmevSRKDTDIILKfnIKDS 491
Cdd:COG4191    225 LELLRPRLKARGIEVELDLPPDLPPVL-GDPGQLEQVLLNLLINAIdamEEGEGGRITIST---RREGDYVVIS--VRDN 298
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237881481  492 GAGINLKDIEHVFDAFcqadgsLTRK--HGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG4191    299 GPGIPPEVLERIFEPF------FTTKpvGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTIT 357
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
338-553 2.18e-34

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 135.74  E-value: 2.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  338 NISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEAdkltLETSKFKLYDLFENLSEN 417
Cdd:COG3852    141 GLAHEIRNPLTGIRGAAQLLERELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRP----PEREPVNLHEVLERVLEL 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  418 LSIfAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIK-FTEYGEVIVTVmEVSRKDTDII------LKFNIKD 490
Cdd:COG3852    217 LRA-EAPKNIRIVRDYDPSLPEVL-GDPDQLIQVLLNLVRNAAEaMPEGGTITIRT-RVERQVTLGGlrprlyVRIEVID 293
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237881481  491 SGAGINLKDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:COG3852    294 NGPGIPEEILDRIFEPF------FTTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRI 350
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
729-838 5.16e-33

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: 125.79  E-value: 5.16e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:COG3706      4 ILVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTA 83
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFS 838
Cdd:COG3706     84 LDDEEDRARALEAGADDYLTKPFDPEELLA 113
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
339-554 4.41e-32

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: 130.47  E-value: 4.41e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHIL------INSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTletsKFKLYDLFE 412
Cdd:COG5000    208 IAHEIKNPLTPIQLSAERLrrkladKLEEDREDLERALDTIIRQVDRLKRIVDEFLDFARLPEPQLE----PVDLNELLR 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  413 NLSENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFTE-YGEVIVTVmevSRKDTDIILKfnIKDS 491
Cdd:COG5000    284 EVLALYEPALKEKDIRLELDLDPDLPEVL-ADRDQLEQVLINLLKNAIEAIEeGGEIEVST---RREDGRVRIE--VSDN 357
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237881481  492 GAGINLKDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG5000    358 GPGIPEEVLERIFEPF------FTTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIR 414
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
443-554 1.08e-31

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


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 119.68  E-value: 1.08e-31
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481   443 GDQTKLNQVLLNIVNNAIKFT-EYGEVIVTVmevsrKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSlTRKHGGT 521
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTpEGGRITVTL-----ERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKR-SRKIGGT 74
                            90       100       110
                    ....*....|....*....|....*....|...
gi 1237881481   522 GLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:smart00387   75 GLGLSIVKKLVELHGGEISVESEPGGGTTFTIT 107
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
318-645 8.25e-31

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 131.78  E-value: 8.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  318 MRLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQR-QHLDKVHKSAESLLSIINNILDFSNIEAD 396
Cdd:PRK09959   698 LEVERNKAINATVAKSQFLATMSHEIRTPISSIMGFLELLSGSGLSKEQRvEAISLAYATGQSLLGLIGEILDVDKIESG 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  397 KLTLETSKFKLYDLFENLSENLSIFAYDKNIELifDIPVALEDIYIG--DQTKLNQVLLNIVNNAIKFTEYGEVIVTVME 474
Cdd:PRK09959   778 NYQLQPQWVDIPTLVQNTCHSFGAIAASKSIAL--SCSSTFPDHYLVkiDPQAFKQVLSNLLSNALKFTTEGAVKITTSL 855
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  475 VSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQAdgSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:PRK09959   856 GHIDDNHAVIKMTIMDSGSGLSQEEQQQLFKRYSQT--SAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGTTFTIT 933
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  555 TQLKIVPN----EPSLQPYINKFKNINTLVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEQasrpFELILMD 630
Cdd:PRK09959   934 IPVEISQQvatvEAKAEQPITLPEKLSILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQH----YDLLITD 1009
                          330
                   ....*....|....*
gi 1237881481  631 WKMSSDNDFKVLEKI 645
Cdd:PRK09959  1010 VNMPNMDGFELTRKL 1024
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
335-551 1.69e-29

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: 120.78  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPMNAIIGLSHILI--NSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSKFKLYDLFE 412
Cdd:TIGR02966  117 FVANVSHELRTPLTVLRGYLETLAdgPDEDPEEWNRALEIMLEQSQRMQSLVEDLLTLSRLESAASPLEDEPVDMPALLD 196
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  413 NLSENLSIFAYDKNIELIFDIPVALeDIYiGDQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRKDTDIILKFNIKDSG 492
Cdd:TIGR02966  197 HLRDEAEALSQGKNHQITFEIDGGV-DVL-GDEDELRSAFSNLVSNAIKYTPEGGTI----TVRWRRDGGGAEFSVTDTG 270
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1237881481  493 AGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEF 551
Cdd:TIGR02966  271 IGIAPEHLPRLTERFYRVDKSRSRDTGGTGLGLAIVKHVLSRHHARLEIESELGKGSTF 329
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
728-842 1.06e-27

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: 108.40  E-value: 1.06e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMI 807
Cdd:cd17548      1 KILIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALT 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17548     81 AYAMKGDREKILEAGCDGYISKPIDTREFLETVAK 115
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
443-559 2.70e-27

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: 107.07  E-value: 2.70e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  443 GDQTKLNQVLLNIVNNAIKFTEY-GEVIVTVmevsrkDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADgslTRKHGGT 521
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKaGEITVTL------SEGGELTLTVEDNGIGIPPEDLPRIFEPFSTAD---KRGGGGT 71
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1237881481  522 GLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLKI 559
Cdd:pfam02518   72 GLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
729-836 1.84e-26

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


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 108.12  E-value: 1.84e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMIA 808
Cdd:COG0745      4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLRA--RPSDIPIIMLTA 81
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:COG0745     82 RDDEEDRVRGLEAGADDYLTKPFDPEEL 109
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
728-844 2.94e-26

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: 107.94  E-value: 2.94e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMI 807
Cdd:COG3437      8 TVLIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLT 87
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWI 844
Cdd:COG3437     88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNAL 124
PRK09303 PRK09303
histidine kinase;
341-554 5.38e-25

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 108.50  E-value: 5.38e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  341 HEIRTPMNA-IIGLSHILIN--SDLNKKQRQHLDKVHKSAESLLSIIN----NILDFSNIEADKLTLETSKFKLYDLFEN 413
Cdd:PRK09303   160 HDLRTPLTAaSLALETLELGqiDEDTELKPALIEQLQDQARRQLEEIErlitDLLEVGRTRWEALRFNPQKLDLGSLCQE 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  414 LSENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFT-EYGEVIVTVME-VSRKdtdiiLKFNIKDS 491
Cdd:PRK09303   240 VILELEKRWLAKSLEIQTDIPSDLPSVY-ADQERIRQVLLNLLDNAIKYTpEGGTITLSMLHrTTQK-----VQVSICDT 313
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  492 GAGINLKDIEHVF-DAFcqadgSLTRKHG--GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:PRK09303   314 GPGIPEEEQERIFeDRV-----RLPRDEGteGYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFT 374
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
729-841 1.02e-24

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: 99.53  E-value: 1.02e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMIA 808
Cdd:pfam00072    1 VLIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIRRR--DPTTPVIILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:pfam00072   79 HGDEDDAVEALEAGADDFLSKPFDPDELLAAIR 111
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
339-563 3.03e-23

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 105.82  E-value: 3.03e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEAdkltletSKFKLYDLFEnLSENL 418
Cdd:PRK11360   397 VAHEIRNPLTAIRGYVQIWRQQTSDPPSQEYLSVVLREVDRLNKVIDQLLEFSRPRE-------SQWQPVSLNA-LVEEV 468
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  419 SIFA----YDKNIELIFDIPVALEDIYIgDQTKLNQVLLNIVNNAIK-FTEYGEVIVTVMEVsrKDTDIILKfnIKDSGA 493
Cdd:PRK11360   469 LQLFqtagVQARVDFETELDNELPPIWA-DPELLKQVLLNILINAVQaISARGKIRIRTWQY--SDGQVAVS--IEDNGC 543
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  494 GINLKDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITtqLKIVPNE 563
Cdd:PRK11360   544 GIDPELLKKIFDPF------FTTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLY--LPINPQG 605
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
335-554 9.91e-23

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 103.18  E-value: 9.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPmnaiigLSHILINSDLNKKQRQHLD-KVHKSAEsLL--------SIINNILDFSNIEADKLTLETSKF 405
Cdd:NF040691   274 FVSDVSHELRTP------LTTIRMAADVIHDSRDDFDpATARSAE-LLhteldrfeSLLSDLLEISRFDAGAAELDVEPV 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  406 KLYDLFENLSENLSIFAYDKNIELIFDIPvALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTvmeVSRKDTDIILK 485
Cdd:NF040691   347 DLRPLVRRVVDALRQLAERAGVELRVDAP-GTPVVAEVDPRRVERVLRNLVVNAIEHGEGKPVVVT---VAQDDTAVAVT 422
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1237881481  486 fnIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:NF040691   423 --VRDHGVGLKPGEVALVFDRFWRADPARARTTGGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRLT 489
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
729-831 3.40e-22

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: 92.19  E-value: 3.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd19920      1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                           90       100
                   ....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd19920     81 LTDTEDKVKGFELGAVDYITKPF 103
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
730-830 7.38e-22

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 91.13  E-value: 7.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMIAN 809
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLRE--LPPDIPVIVLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1237881481  810 TMLADKNKALDCGMNDYIEKP 830
Cdd:cd00156     79 ADEEDAVRALELGADDYLVKP 99
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
730-830 1.02e-21

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: 90.54  E-value: 1.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMIAN 809
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLRE--KGSDIPIIMLTAK 78
                           90       100
                   ....*....|....*....|.
gi 1237881481  810 TMLADKNKALDCGMNDYIEKP 830
Cdd:cd17574     79 DEEEDKVLGLELGADDYITKP 99
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
317-558 1.99e-21

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: 98.02  E-value: 1.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  317 RMRLAKIQAEKANeTKTHFLNNISHEIRTPMNAIIGLSHILINSDL-NKKQRQH----LDKVHKsAESllsIINNILDFS 391
Cdd:COG5806    187 LLRKELQRAEKLE-VVSELAASIAHEVRNPLTVVRGFIQLLQEPELsDEKRKQYiriaLEELDR-AEA---IITDYLTFA 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  392 NIEADKLTletsKFKLYDLFENLSENLSIFAYDKNIELIFDIPvalEDIYI-GDQTKLNQVLLNIVNNAIKFTEYGEViV 470
Cdd:COG5806    262 KPQPEKLE----KIDVSEELEHVIDVLSPYANMNNVEIQTELE---PGLYIeGDRQKLQQCLINIIKNGIEAMPNGGT-L 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  471 TVmEVSRKDTDIILKfnIKDSGAGINLKDIEHVfdafcqadGSL--TRKHGGTGLGLAISQKFIELMGGEIWVESEVGKG 548
Cdd:COG5806    334 TI-DVSIDKNKVIIS--IKDTGVGMTKEQLERL--------GEPyfSTKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKG 402
                          250
                   ....*....|
gi 1237881481  549 SEFNITTQLK 558
Cdd:COG5806    403 TTFTITLPLA 412
HPtr COG2198
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
272-977 3.12e-21

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


Pssm-ID: 441800 [Multi-domain]  Cd Length: 871  Bit Score: 100.12  E-value: 3.12e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  272 QLLLYKNRFNLNPLLPLLSSIFIISLLILIYIIQKSTSSIVSMSSRMRLAKIQAEKANETKTHFLNNISHEIRTPMNAII 351
Cdd:COG2198    173 VLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLLLL 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  352 GLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKLTLETSKFKLYDLFENLSENLSIFAYDKNIELIF 431
Cdd:COG2198    253 LLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLLLL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  432 DIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQAD 511
Cdd:COG2198    333 LLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSLLL 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  512 GSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLKIVPNEPSLQPYINKFKNINTLVINESMAVKNII 591
Cdd:COG2198    413 LLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLL 492
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  592 TQMLREFGMMVTSAESGYDALSIFSSEQASRPFELILMDWKMSSDNDFKVLEKIHYLVTTNNYMRPKIILVTDYGQEEFD 671
Cdd:COG2198    493 LLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGLLL 572
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  672 LVTNDLGVDAFVNKPVTPYNMAKSLLIAFNESLNDITHHLPETNNLNNMTKLLAGSNILLVEDNEINSEVTSSLLSLHKI 751
Cdd:COG2198    573 GGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 652
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  752 NVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIANTMLADKNKALDCGMNDYIEKPF 831
Cdd:COG2198    653 AVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLLLL 732
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  832 NINKLFSIMRKWITPSKPEIFTSLSEQENInlshnsniINFQvGLEICSGSVSLYQKLLKKFADSECDFLQRFENLILEK 911
Cdd:COG2198    733 LLLLLLLLLLLLLAAAAAAAASPAAPALPV--------LDLE-ALRRLGGDPELLRELLELFLEELPELLAELRQALAAG 803
                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  912 NRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQetDDNLIKQVKLIDEKIFEVIELISQL 977
Cdd:COG2198    804 DLEALARLAHKLKGSAGNLGAPRLAELAAELEQAARAGD--LEEAEELLAELEAELERVLAALEAL 867
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
729-839 2.15e-20

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: 87.51  E-value: 2.15e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17580      1 ILVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTG 80
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSI 839
Cdd:cd17580     81 YGQPEDRERALEAGFDAHLVKPVDPDELIEL 111
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
319-539 8.30e-20

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 93.74  E-value: 8.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  319 RLAKIqAEKANETKTHFLNNISHEIRTPMnAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEADKL 398
Cdd:NF012163   228 QLAST-LEKNEQMRRDFMADISHELRTPL-AVLRAELEAIQDGIRKFTPESLDSLQAEVGTLTKLVDDLHDLSMSDEGAL 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  399 TLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALedIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRK 478
Cdd:NF012163   306 AYQKASVDLVPLLEVEGGAFRERFASAGLELEVSLPDSS--LVFGDRDRLMQLFNNLLENSLRYTDSGGSL----HISAS 379
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  479 DTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEI 539
Cdd:NF012163   380 QRPKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRASGGSGLGLAISLNIVQAHGGTL 440
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
729-831 1.60e-19

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 84.47  E-value: 1.60e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17538      2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITA 81
                           90       100
                   ....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd17538     82 LDDREDRIRGLEAGADDFLSKPI 104
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
334-564 4.09e-19

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 91.77  E-value: 4.09e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  334 HFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVH-KSAESLLSIINNILDFSniEADKLTLETSKfkLYDLFE 412
Cdd:PRK10364   239 HLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMaKEADRLNRVVSELLELV--KPTHLALQAVD--LNDLIN 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  413 NLSENLSIFAYDKNIELIFDIPVALEDIYIgDQTKLNQVLLNIVNNAIK-FTEYGEVIVTVMEVSRKdtdiiLKFNIKDS 491
Cdd:PRK10364   315 HSLQLVSQDANSREIQLRFTANDTLPEIQA-DPDRLTQVLLNLYLNAIQaIGQHGVISVTASESGAG-----VKISVTDS 388
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1237881481  492 GAGINLKDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLKIVPNEP 564
Cdd:PRK10364   389 GKGIAADQLEAIFTPY------FTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPVNITRRDP 455
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
728-842 5.44e-19

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: 90.79  E-value: 5.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMI 807
Cdd:COG2204      4 RILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELRAL--DPDLPVILLT 81
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:COG2204     82 GYGDVETAVEAIKAGAFDYLTKPFDLEELLAAVER 116
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
727-832 2.14e-18

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: 81.72  E-value: 2.14e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVEDNEINSEVTSSLL-SLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIA 805
Cdd:cd17551      1 MRILIVDDNPTNLLLLEALLrSAGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVM 80
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFN 832
Cdd:cd17551     81 ITADTDREVRLRALEAGATDFLTKPFD 107
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
444-553 2.39e-18

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: 81.38  E-value: 2.39e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIIlkfNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGL 523
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRLNRFLL---TVSDSGPGIPPNLREEIFERFRQGDGSSTRAHGGTGL 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  524 GLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:cd16925     78 GLSIVKEFVELHGGTVTVSDAPGGGALFQV 107
PRK10490 PRK10490
sensor protein KdpD; Provisional
320-562 4.61e-18

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 90.10  E-value: 4.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  320 LAKIQAEKaNETKTHFLNNISHEIRTPMNAIIGLSHILInSDLNKKQRQHLDKVHKSAESLLS---IINNILDFSNIEAD 396
Cdd:PRK10490   653 QARLASER-EQLRNALLAALSHDLRTPLTVLFGQAEILT-LDLASEGSPHARQASEIRQQVLNttrLVNNLLDMARIQSG 730
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  397 KLTLETSKFKLYDLFENLSENLSIFAYDKNIELifDIPVALEDIYIgDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVS 476
Cdd:PRK10490   731 GFNLRKEWLTLEEVVGSALQMLEPGLSGHPINL--SLPEPLTLIHV-DGPLFERVLINLLENAVKYAGAQAEIGIDAHVE 807
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDtdiiLKFNIKDSGAGINLKDIEHVFDAFCQADgsltrKHG---GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:PRK10490   808 GER----LQLDVWDNGPGIPPGQEQLIFDKFARGN-----KESaipGVGLGLAICRAIVEVHGGTIWAENRPEGGACFRV 878

                   ....*....
gi 1237881481  554 TTQLKIVPN 562
Cdd:PRK10490   879 TLPLETPPE 887
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
335-547 6.65e-18

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: 87.83  E-value: 6.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPMNAIIGLSHILINSDlnKKQRQHLDKVHKSAESL--LS-IINNILDFSNIEADKLTLETSKFKLYDLF 411
Cdd:TIGR01386  244 FSADLAHELRTPLTNLLGQTQVALSQP--RTGEEYREVLESNLEELerLSrMVSDMLFLARADNGQLALERVRLDLAAEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  412 ENLSENLSIFAYDKNIELIFDIPVALEdiyiGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIilkfNIKDS 491
Cdd:TIGR01386  322 AKVAEYFEPLAEERGVRIRVEGEGLVR----GDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRV----SVSNP 393
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  492 GAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGK 547
Cdd:TIGR01386  394 GPGIPPEHLSRLFDRFYRVDPARSNSGEGTGLGLAIVRSIMEAHGGRASAESPDGK 449
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
728-844 9.11e-18

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 80.78  E-value: 9.11e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKI--NVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIA 805
Cdd:COG4565      5 RVLIVEDDPMVAELLRRYLERLPGfeVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELRAR--GPDVDVIV 82
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWI 844
Cdd:COG4565     83 ITAARDPETVREALRAGVVDYLIKPFTFERLREALERYL 121
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
317-599 1.15e-17

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


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 88.45  E-value: 1.15e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  317 RMRLAKIQAEKANETKTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEAD 396
Cdd:PRK10618   435 KLQQAQREYEKNQQARKAFLQNIGDELKQPLQSLAQLAAQLRQTSDEEQQQPELDQLAEQSDVLVRLVDNIQLLNMLETQ 514
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  397 KLTLETSKFKLYDLFENLSENLSIFAYDKNIELIFDIPVALEDIYIGDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMevS 476
Cdd:PRK10618   515 DWKPEQELFSLQDLIDEVLPEVLPAIKRKGLQLLIHNHLKAEQLRIGDRDALRKILLLLLNYAITTTAYGKITLEVD--Q 592
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILKFNIKDSGAGINLKDIE---HVFDAFCQADgsltrKHG-GTGLGLAISQKFIELMGGEIWVESEVGKGSEFN 552
Cdd:PRK10618   593 DESSPDRLTIRILDTGAGVSIKELDnlhFPFLNQTQGD-----RYGkASGLTFFLCNQLCRKLGGHLTIKSREGLGTRYS 667
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1237881481  553 ITtqLKIVPNEPSLQPYINK-FKNINTLVINESMAVKNIITQMLREFG 599
Cdd:PRK10618   668 IH--LKMLAADPEVEEEEEKlLDGVTVLLDITSEEVRKIVTRQLENWG 713
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-553 1.57e-17

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: 79.00  E-value: 1.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIK-FTEYGEVIVTVMEVSRKdtdiiLKFNIKDSGAGINLKDIEHVFDAFCQadgslTRKHG-GTGLGL 525
Cdd:cd16943      4 LNQVLLNLLVNAAQaMEGRGRITIRTWAHVDQ-----VLIEVEDTGSGIDPEILGRIFDPFFT-----TKPVGeGTGLGL 73
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  526 AISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:cd16943     74 SLSYRIIQKHGGTIRVASVPGGGTRFTI 101
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-554 1.63e-17

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


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 78.91  E-value: 1.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVivTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAI 527
Cdd:cd16921      1 LGQVLTNLLGNAIKFRRPRRP--PRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSR--EEYEGTGVGLAI 76
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  528 SQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16921     77 VRKIIERHGGRIWLESEPGEGTTFYFT 103
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
332-395 2.38e-17

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


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 77.22  E-value: 2.38e-17
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481   332 KTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEA 395
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYLELLLDTELSEEQREYLETILREAERLLRLINDLLDLSRIEA 65
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
332-395 4.85e-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: 76.10  E-value: 4.85e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  332 KTHFLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEA 395
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYLELLRDEKLDEEQREYLETILRSAERLLRLINDLLDLSRIEA 65
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
335-563 5.19e-17

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 84.68  E-value: 5.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPMNAIIGLSHILINSDLNKKQRqhlDKVHKSAESLL----SIINNILDFSNIEADKLTLETSKFK---L 407
Cdd:PRK11006   207 FFANVSHELRTPLTVLQGYLEMMQDQPLEGALR---EKALHTMREQTqrmeGLVKQLLTLSKIEAAPTIDLNEKVDvpmM 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  408 YDLFENLSENLSifayDKNIELIFDIPVALEdiYIGDQTKLNQVLLNIVNNAIKFTEYGevivTVMEVSRKDTDIILKFN 487
Cdd:PRK11006   284 LRVLEREAQTLS----QGKHTITFEVDNSLK--VFGNEDQLRSAISNLVYNAVNHTPEG----THITVRWQRVPQGAEFS 353
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  488 IKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLK-IVPNE 563
Cdd:PRK11006   354 VEDNGPGIAPEHIPRLTERFYRVDKARSRQTGGSGLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPERlIAKNS 430
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
730-836 6.14e-17

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: 77.65  E-value: 6.14e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIAN 809
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGI--ETPVLLLTAL 78
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  810 TMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17625     79 DAVEDRVKGLDLGADDYLPKPFSLAEL 105
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
729-841 9.44e-17

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: 77.04  E-value: 9.44e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEinsEVTSSL---LSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIA 805
Cdd:cd17627      1 ILVVDDDR---AVRESLrrsLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAAGN--DLPILV 75
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17627     76 LTARDSVSDRVAGLDAGADDYLVKPFALEELLARVR 111
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
339-553 1.11e-16

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 85.50  E-value: 1.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHILINS-DLNKKQRQHLDKVHKSAESLLSIINNILDFSNieadKLTLETSKFKLYDLFENLSEN 417
Cdd:PRK13837   457 IAHNFNNILGAILGYAEMALNKlARHSRAARYIDEIISAGARARLIIDQILAFGR----KGERNTKPFDLSELVTEIAPL 532
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  418 LSIfAYDKNIELIFDIPvALEDIYIGDQTKLNQVLLNIVNNAIK-FTEYG--EVIVTVMEVSRKDT---------DIILk 485
Cdd:PRK13837   533 LRV-SLPPGVELDFDQD-QEPAVVEGNPAELQQVLMNLCSNAAQaMDGAGrvDISLSRAKLRAPKVlshgvlppgRYVL- 609
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881481  486 FNIKDSGAGINLKDIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:PRK13837   610 LRVSDTGAGIDEAVLPHIFEPF------FTTRAGGTGLGLATVHGIVSAHAGYIDVQSTVGRGTRFDV 671
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
422-554 5.13e-16

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


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 81.43  E-value: 5.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  422 AYDKNIELIFDIPVALEDIYIgDQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFNIKDSGAGINLKDIE 501
Cdd:COG3290    257 ARERGIDLTIDIDSDLPDLPL-SDTDLVTILGNLLDNAIEAVEKLPEEERRVELSIRDDGDELVIEVEDSGPGIPEELLE 335
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1237881481  502 HVFDafcqaDGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:COG3290    336 KIFE-----RGFSTKLGEGRGLGLALVKQIVEKYGGTIEVESEEGEGTVFTVR 383
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
339-558 7.92e-16

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: 81.70  E-value: 7.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPMNAIIGLSHILinsdLNKKQRQHldKVHKSAESLLSIINNIL-DFSNIEADKlTLETSKFKLYDLFENLSEN 417
Cdd:COG5805    294 IAHEIRNPLTSIKGFLQLL----QPGIEDKE--EYFDIMLSELDRIESIIsEFLALAKPQ-AVNKEKENINELIQDVVTL 366
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  418 LSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKFTEYGEVIVtvMEVSRKDTDIILKfnIKDSGAGINL 497
Cdd:COG5805    367 LETEAILHNIQIRLELLDEDPFIY-CDENQIKQVFINLIKNAIEAMPNGGTIT--IHTEEEDNSVIIR--VIDEGIGIPE 441
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  498 KDIEHVFDAFCqadgslTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNITTQLK 558
Cdd:COG5805    442 ERLKKLGEPFF------TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPLS 496
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
332-554 1.23e-15

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


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 80.97  E-value: 1.23e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  332 KTHFLNNISHEIRTPMNAIIGLSHILINSdlNKKQRQHLDKVHKSAES---LLSIINNILDFSNIEADKLTLETSKF--- 405
Cdd:PRK09835   262 QSNFSADIAHEIRTPITNLITQTEIALSQ--SRSQKELEDVLYSNLEEltrMAKMVSDMLFLAQADNNQLIPEKKMLdla 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  406 ----KLYDLFENLSEnlsifayDKNIELIFD-IPVALEdiyiGDQTKLNQVLLNIVNNAIKFTEYGEVIVtvmeVSRKDT 480
Cdd:PRK09835   340 devgKVFDFFEAWAE-------ERGVELRFVgDPCQVA----GDPLMLRRAISNLLSNALRYTPAGEAIT----VRCQEV 404
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  481 DIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVgKGSEFNIT 554
Cdd:PRK09835   405 DHQVQLVVENPGTPIAPEHLPRLFDRFYRVDPSRQRKGEGSGIGLAIVKSIVVAHKGTVAVTSDA-RGTRFVIS 477
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
444-546 1.38e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli 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: 73.65  E-value: 1.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGL 523
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKL----RIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRASGGSGL 76
                           90       100
                   ....*....|....*....|....
gi 1237881481  524 GLAISQKFIELMGGEIWVE-SEVG 546
Cdd:cd16946     77 GLAICHNIALAHGGTISAEhSPLG 100
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
729-841 2.10e-15

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: 73.29  E-value: 2.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQ--SLPVLILTA 78
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17624     79 RDGVDDRVAGLDAGADDYLVKPFALEELLARLR 111
PRK10604 PRK10604
sensor protein RstB; Provisional
331-551 2.73e-15

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 79.65  E-value: 2.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  331 TKTHFLNNISHEIRTPmnaIIGLSHILINSD-LNKKQRQHLDKVHKSAESLlsiINNILDFSNIEADKLTLETSKFklyD 409
Cdd:PRK10604   211 SKKQLIDGIAHELRTP---LVRLRYRLEMSDnLSAAESQALNRDIGQLEAL---IEELLTYARLDRPQNELHLSEP---D 281
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  410 LFENLSENLSIFAY---DKNIELifDIPVAlEDIYIGDQTKLNQVLLNIVNNAIKFTEyGEVIVTVmevSRKDTDIILKf 486
Cdd:PRK10604   282 LPAWLSTHLADIQAvtpEKTVRL--DTPHQ-GDYGALDMRLMERVLDNLLNNALRYAH-SRVRVSL---LLDGNQACLI- 353
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  487 nIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVE-SEVGkGSEF 551
Cdd:PRK10604   354 -VEDDGPGIPPEERERVFEPFVRLDPSRDRATGGCGLGLAIVHSIALAMGGSVNCDeSELG-GARF 417
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-554 4.33e-15

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


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 72.04  E-value: 4.33e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIK-----FTEYGEVIVTVMevsrKDTDIILKFNIKDSGAGINLKDIEHVFDAFcqadgsLTRKHGGTG 522
Cdd:cd16920      1 IQQVLINLVRNGIEamsegGCERRELTIRTS----PADDRAVTISVKDTGPGIAEEVAGQLFDPF------YTTKSEGLG 70
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1237881481  523 LGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16920     71 MGLSICRSIIEAHGGRLSVESPAGGGATFQFT 102
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
729-836 6.30e-15

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: 72.05  E-value: 6.30e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRER--FDGVLMDCQMPVMDGYKATQVIRKELNLSELP-IIA 805
Cdd:cd19933      3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEhsFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIVA 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd19933     83 LTANTDDSTREKCLSLGMNGVITKPVSLHAL 113
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
727-841 8.73e-15

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: 71.51  E-value: 8.73e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAM 806
Cdd:cd17618      1 RTILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIML 80
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17618     81 TARGEEEDKVRGLEAGADDYITKPFSPRELVARIK 115
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
728-830 8.77e-15

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: 70.96  E-value: 8.77e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHK--INVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIA 805
Cdd:COG4753      1 KVLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIREL--DPDTKIII 78
                           90       100
                   ....*....|....*....|....*
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKP 830
Cdd:COG4753     79 LSGYSDFEYAQEAIKLGADDYLLKP 103
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-554 1.83e-14

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: 70.43  E-value: 1.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEygevivTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAI 527
Cdd:cd16949      1 LARALENVLRNALRYSP------SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDRESGGTGLGLAI 74
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  528 SQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16949     75 AERAIEQHGGKIKASNRKPGGLRVRIW 101
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
729-842 2.96e-14

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 76.43  E-value: 2.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMIA 808
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSH--ETRTPVILMTA 84
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:PRK11361    85 YAEVETAVEALRCGAFDYVIKPFDLDELNLIVQR 118
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
728-837 4.18e-14

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


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 69.67  E-value: 4.18e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLS-LHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAM 806
Cdd:cd19923      2 KVLVVDDFSTMRRIIKNLLKeLGFNNVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMV 81
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFN-------INKLF 837
Cdd:cd19923     82 TAEAKKENVIAAAQAGVNNYIVKPFTaatlkekLEKIF 119
orf27 CHL00148
Ycf27; Reviewed
729-836 4.33e-14

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 73.21  E-value: 4.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:CHL00148     9 ILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKE---SDVPIIMLTA 85
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:CHL00148    86 LGDVSDRITGLELGADDYVVKPFSPKEL 113
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
326-542 4.39e-14

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 75.83  E-value: 4.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  326 EKANETKTHFLNNISHEIRTPMNAIIGlshilinsDLNKKQrqhlDKVHK-SAESLLSI----------INNILDFSNIE 394
Cdd:PRK10549   234 EKNEQMRRDFMADISHELRTPLAVLRG--------ELEAIQ----DGVRKfTPESVASLqaevgtltklVDDLHQLSLSD 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  395 ADKLTLETSKFKLYDLFEnlsenLSIFAY-----DKNIELIFDIPvaLEDIYIGDQTKLNQVLLNIVNNAIKFT-EYGEV 468
Cdd:PRK10549   302 EGALAYRKTPVDLVPLLE-----VAGGAFrerfaSRGLTLQLSLP--DSATVFGDPDRLMQLFNNLLENSLRYTdSGGSL 374
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  469 IVTVmeVSRKDTDIIlkfNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVE 542
Cdd:PRK10549   375 HISA--EQRDKTLRL---TFADSAPGVSDEQLQKLFERFYRTEGSRNRASGGSGLGLAICLNIVEAHNGRIIAA 443
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
336-542 5.24e-14

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 75.74  E-value: 5.24e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  336 LNNISHEIRTPmnaiigLSHI-LINSDLNKKQ--RQHLDKVHKSAESLLSIINNILDFSNIEAdKLTLETSKFKLYDLFE 412
Cdd:PRK09470   247 LSDISHELRTP------LTRLqLATALLRRRQgeSKELERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSLWS 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  413 NLSENLSIFAYDKNIELIFDIPVALEDIYiGDQTKLNQVLLNIVNNAIKfteYGEVIVTVMEVSRKDTDIILkfnIKDSG 492
Cdd:PRK09470   320 EVLEDAKFEAEQMGKSLTVSAPPGPWPIN-GNPNALASALENIVRNALR---YSHTKIEVAFSVDKDGLTIT---VDDDG 392
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1237881481  493 AGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVE 542
Cdd:PRK09470   393 PGVPEEEREQIFRPFYRVDEARDRESGGTGLGLAIVENAIQQHRGWVKAE 442
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
437-550 6.32e-14

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: 68.97  E-value: 6.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  437 LEDIYI-GDQTKLNQVLLNIVNNAIKFTEYGEVIVtvMEVSRKDTDIILkfnIKDSGAGINLKDIEHVFDAFCQADGSLT 515
Cdd:cd16940      2 AADIQVqGDALLLFLLLRNLVDNAVRYSPQGSRVE--IKLSADDGAVIR---VEDNGPGIDEEELEALFERFYRSDGQNY 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  516 rkhGGTGLGLAISQKFIELMGGEIWVESEVGKGSE 550
Cdd:cd16940     77 ---GGSGLGLSIVKRIVELHGGQIFLGNAQGGGLE 108
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
431-554 6.92e-14

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: 69.46  E-value: 6.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  431 FDIPVALED--IY-IGDQTKLNQVLLNIVNNAIKFTEYGEVIVtvMEVSRKDTDIILkfNIKDSGAGINLKDIEHVFDAF 507
Cdd:cd16947      1 FQVEINIPDrpIYaNANTEALQRILKNLISNAIKYGSDGKFLG--MTLREDEKHVYI--DIWDKGKGISETEKDHVFERL 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1237881481  508 CQADGSLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16947     77 YTLEDSRNSAKQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVT 123
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
329-391 7.08e-14

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


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 67.24  E-value: 7.08e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  329 NETKTHFLNNISHEIRTPMNAIIGLSHILINSDL-NKKQRQHLDKVHKSAESLLSIINNILDFS 391
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLdDEEQREYLERIREEAERLLRLINDLLDLS 64
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
730-836 2.27e-13

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: 67.68  E-value: 2.27e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIAN 809
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAK 80
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  810 TMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd19937     81 GEEFDKVLGLELGADDYITKPFSPREL 107
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
341-548 2.84e-13

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 73.34  E-value: 2.84e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  341 HEIRTPMNAIIGLSHILInSDLNKKQRQH-LDKVHKSAESLLSIINNILDFSNIEADKLTLETSKFKLYDLFENLSENLS 419
Cdd:PRK11100   265 HELKSPLAAIRGAAELLQ-EDPPPEDRARfTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAALLEELVEARE 343
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  420 IFAYDKNIELIFDIPvaleDIYI-GDQTKLNQVLLNIVNNAIKFT-EYGEVIVTVmevSRKDTDIILkfNIKDSGAGINL 497
Cdd:PRK11100   344 AQAAAKGITLRLRPD----DARVlGDPFLLRQALGNLLDNAIDFSpEGGTITLSA---EVDGEQVAL--SVEDQGPGIPD 414
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1237881481  498 KDIEHVFDAFCqadgSLTRKHGG---TGLGLAISQKFIELMGGEIWVESEVGKG 548
Cdd:PRK11100   415 YALPRIFERFY----SLPRPANGrksTGLGLAFVREVARLHGGEVTLRNRPEGG 464
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
729-837 3.02e-13

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: 67.16  E-value: 3.02e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRER-FDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMI 807
Cdd:cd17544      3 VLVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHPdIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGIS 82
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  808 A---NTMLAdknKALDCGMNDYIEKPFNINKLF 837
Cdd:cd17544     83 AsgdNALSA---RFIKAGANDFLTKPFLPEEFY 112
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
729-842 3.15e-13

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


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 67.33  E-value: 3.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17562      3 ILAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILMLTT 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17562     83 ESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKK 116
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
444-554 4.56e-13

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: 66.54  E-value: 4.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFTEYGEVIVTVMEvsRKDTDIILKfnIKDSGAGINLKDIEHVFDA-FCQADGSLTRKhgGTG 522
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSE--TNEQGVVLS--IKDFGIGIPEEDLPRVFDKgFTGENGRNFQE--STG 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1237881481  523 LGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16948     76 MGLYLVKKLCDKLGHKIDVESEVGEGTTFTIT 107
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
729-841 6.06e-13

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: 66.17  E-value: 6.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKT---SQVPVLMLTA 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17623     78 RGDDIDRILGLELGADDYLPKPFNPRELVARIR 110
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
729-838 9.26e-13

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: 65.81  E-value: 9.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17598      1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFS 838
Cdd:cd17598     81 LSDPRDVIRGLECGADNFITKPYDEKYLLS 110
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
728-830 5.66e-12

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: 63.95  E-value: 5.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSL---HKInVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPII 804
Cdd:cd17541      2 RVLIVDDSAVMRKLLSRILESdpdIEV-VGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEALRRIMAE---RPTPVV 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  805 aMIanTMLADKN-----KALDCGMNDYIEKP 830
Cdd:cd17541     78 -MV--SSLTEEGaeitlEALELGAVDFIAKP 105
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
728-836 6.40e-12

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: 63.17  E-value: 6.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMI 807
Cdd:cd17619      2 HILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELREQ---SEVGIILVT 78
                           90       100
                   ....*....|....*....|....*....
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17619     79 GRDDEVDRIVGLEIGADDYVTKPFNPREL 107
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
729-836 1.11e-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: 62.83  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVRKT---SNVPIIMLTA 77
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17614     78 KDSEVDKVLGLELGADDYVTKPFSNREL 105
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
728-841 1.25e-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: 62.82  E-value: 1.25e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTssLLSLHKINVTCAI----NGKDALLKLQRE-------RFDGVLMDCQMPVMDGYKATQVIRKEL 796
Cdd:cd17557      1 TILLVEDNPGDAELI--QEAFKEAGVPNELhvvrDGEEALDFLRGEgeyadapRPDLILLDLNMPRMDGFEVLREIKADP 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1237881481  797 NLSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17557     79 DLRRIPVVVLTTSDAEEDIERAYELGANSYIVKPVDFEEFVEAIR 123
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
579-689 1.30e-11

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: 64.16  E-value: 1.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseqASRPFELILMDWKMSSDNDFKVLEKIHylvTTNNYMRPK 658
Cdd:COG3706      5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELL----QEHRPDLILLDLEMPDMDGLELCRRLR---ADPRTADIP 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:COG3706     78 IIFLTALDDEEDRARALEAGADDYLTKPFDP 108
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
753-845 1.33e-11

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


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 62.50  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  753 VTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIR--KELNlSELPIIAMIANTMLADKNKALDCGMNDYIEKP 830
Cdd:COG5803     29 VFQAANGKEALEKVKELKPDLVLLDMKMPGMDG---IEILKeiKEID-PDIPVIMMTAYGELDMVEEAKELGAKGYFTKP 104
                           90
                   ....*....|....*
gi 1237881481  831 FNINKLFSIMRKWIT 845
Cdd:COG5803    105 FDIDELREAVNKLLK 119
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
727-841 1.85e-11

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: 62.10  E-value: 1.85e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAM 806
Cdd:cd17626      1 ARILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIRAE---SGVPIVML 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17626     78 TAKSDTVDVVLGLESGADDYVAKPFKPKELVARIR 112
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
729-830 2.32e-11

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: 61.83  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMIA 808
Cdd:cd17555      3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQITKE--SPDTPVIVVSG 80
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17555     81 AGVMSDAVEALRLGAWDYLTKP 102
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
729-836 2.44e-11

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: 61.88  E-value: 2.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKL--QRERFDGVLMDCQMPVMDGYKATQVIRKELnlsELPIIAM 806
Cdd:cd17584      1 VLVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLreNKDEFDLVITDVHMPDMDGFEFLELIRLEM---DLPVIMM 77
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17584     78 SADGSTSTVMKGLAHGACDYLLKPVSIEDL 107
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-554 2.61e-11

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: 61.29  E-value: 2.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEygevivTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAI 527
Cdd:cd16939      1 MARALDNLLRNALRYAH------RTVRIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRATGGFGLGLAI 74
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  528 SQKFIELMGGEIWV-ESEVGkGSEFNIT 554
Cdd:cd16939     75 VHRVALWHGGHVECdDSELG-GACFRLT 101
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
720-841 2.82e-11

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: 63.82  E-value: 2.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  720 MTKLlagsNILLVEDNEINSEVTSSLLSLHKINV-TCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnl 798
Cdd:COG3707      1 MRGL----RVLVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE--- 73
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1237881481  799 SELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:COG3707     74 RPAPVILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALE 116
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
729-830 3.44e-11

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: 60.67  E-value: 3.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSELPIIAMIA 808
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSG---TEVCRQLRARSNVPVIMVTA 77
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17621     78 KDSEIDKVVGLELGADDYVTKP 99
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
729-830 3.53e-11

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


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 60.85  E-value: 3.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd19927     81 KGMTSDRIKGYNAGCDGYLSKP 102
PRK11517 PRK11517
DNA-binding response regulator HprR;
729-841 3.55e-11

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 64.15  E-value: 3.55e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRkelNLSELPIIAMIA 808
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLR---TAKQTPVICLTA 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:PRK11517    80 RDSVDDRVRGLDSGANDYLVKPFSFSELLARVR 112
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
729-830 4.89e-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: 60.86  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQ---------RERFDGVLMDCQMPVMDGYKATQVIRKELNLS 799
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLEnlakegndlSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  800 ELPIiamIANTMLA---DKNKALDCGMNDYIEKP 830
Cdd:cd19924     81 NIPV---ILNSSLSgefSRARGKKVGADAYLAKF 111
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
730-841 5.06e-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: 60.83  E-value: 5.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEIN-SEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:cd17615      2 VLVVDDEPNiTELLSMALRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGP--DVPVLFLTA 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17615     80 KDSVEDRIAGLTAGGDDYVTKPFSLEEVVARLR 112
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
729-781 1.18e-10

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


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 57.58  E-value: 1.18e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1237881481   729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMP 781
Cdd:smart00448    3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
729-836 1.21e-10

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: 59.60  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelnLSELPIIAMIA 808
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIRQ---ISNVPIIFISS 77
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd18159     78 RDDNMDQVMAINMGGDDYITKPFDLDVL 105
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
729-836 1.42e-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: 59.87  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSslLSLHKI---NVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIA 805
Cdd:cd17552      4 ILVIDDEEDIREVVQ--ACLEKLagwEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVIL 81
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17552     82 LTAKAQPSDRQRFASLGVAGVIAKPFDPLTL 112
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
729-831 1.88e-10

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: 59.31  E-value: 1.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSELPIIAMIA 808
Cdd:cd19939      2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDG---LTVCREVREHSHVPILMLTA 78
                           90       100
                   ....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd19939     79 RTEEMDRVLGLEMGADDYLCKPF 101
PRK13557 PRK13557
histidine kinase; Provisional
444-694 1.96e-10

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 64.69  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFTEYGEViVTV----MEVSRKDTDIILKF--------NIKDSGAGINLKDIEHVFDAFCQad 511
Cdd:PRK13557   274 DPTQAEVALLNVLINARDAMPEGGR-VTIrtrnVEIEDEDLAMYHGLppgryvsiAVTDTGSGMPPEILARVMDPFFT-- 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  512 gslTRKHG-GTGLGLAISQKFIELMGGEIWVESEVGKGSE----FNITTQLKIVPNEPSLQPyINKFKNINTLVINESMA 586
Cdd:PRK13557   351 ---TKEEGkGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTvrlyFPASDQAENPEQEPKARA-IDRGGTETILIVDDRPD 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  587 VKNIITQMLREFGMMVTSAESGYDALSIFSSEqasRPFELILMDWKMSSDNDFKVLE--------KIHYLVTTnNYMRPK 658
Cdd:PRK13557   427 VAELARMILEDFGYRTLVASNGREALEILDSH---PEVDLLFTDLIMPGGMNGVMLArearrrqpKIKVLLTT-GYAEAS 502
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1237881481  659 IILvTDYGQEEFDLvtndlgvdafVNKPVTPYNMAK 694
Cdd:PRK13557   503 IER-TDAGGSEFDI----------LNKPYRRAELAR 527
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
729-842 2.24e-10

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: 59.00  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:cd17594      2 VLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRAR---SDVPIIIISG 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  809 NTML-ADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17594     79 DRRDeIDRVVGLELGADDYLAKPFGLRELLARVRA 113
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-551 2.46e-10

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


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 58.75  E-value: 2.46e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFT-EYGEVIVTVMEVSRKdtdiiLKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLA 526
Cdd:cd16952      1 LRSAFSNLVSNAVKYTpPSDTITVRWSQEESG-----ARLSVEDTGPGIPPEHIPRLTERFYRVDIERCRNTGGTGLGLA 75
                           90       100
                   ....*....|....*....|....*
gi 1237881481  527 ISQKFIELMGGEIWVESEVGKGSEF 551
Cdd:cd16952     76 IVKHVMSRHDARLLIASELGKGSRF 100
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
729-836 2.77e-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: 58.83  E-value: 2.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDN-EINSEVTSSLLSLHKInVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElNLSeLPIIAMI 807
Cdd:cd19934      1 LLLVEDDaLLAAQLKEQLSDAGYV-VDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSE-GRA-TPVLILT 77
                           90       100
                   ....*....|....*....|....*....
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd19934     78 ARDSWQDKVEGLDAGADDYLTKPFHIEEL 106
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
454-554 2.92e-10

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: 58.45  E-value: 2.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  454 NIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAfcqadGSLTRKHGGTGLGLAISQKFIE 533
Cdd:cd16915      7 NLIDNALDALAATGAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFER-----GVSTKGQGERGIGLALVRQSVE 81
                           90       100
                   ....*....|....*....|.
gi 1237881481  534 LMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16915     82 RLGGSITVESEPGGGTTFSIR 102
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
579-689 3.03e-10

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: 61.33  E-value: 3.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseqASRPFELILMDWKMSSDNDFKVLEKIHylvTTNNYMRPK 658
Cdd:COG3437     10 LIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELL----LEAPPDLILLDVRMPGMDGFELLRLLR---ADPSTRDIP 82
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:COG3437     83 VIFLTALADPEDRERALEAGADDYLTKPFDP 113
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
579-686 3.18e-10

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: 58.01  E-value: 3.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEqasrPFELILMDWKMSSDNDFKVLEKIHylvttNNYMRPK 658
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREE----RPDLVLLDLMMPGMDGLELLRKLR-----ELPPDIP 71
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKP 686
Cdd:cd00156     72 VIVLTAKADEEDAVRALELGADDYLVKP 99
PhoB TIGR02154
phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response ...
725-847 4.37e-10

phosphate regulon transcriptional regulatory protein PhoB; PhoB is a DNA-binding response regulator protein acting with PhoR in a 2-component system responding to phosphate ion. PhoB acts as a positive regulator of gene expression for phosphate-related genes such as phoA, phoS, phoE and ugpAB as well as itself. It is often found proximal to genes for the high-affinity phosphate ABC transporter (pstSCAB; GenProp0190) and presumably regulates these as well. [Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 131209 [Multi-domain]  Cd Length: 226  Bit Score: 60.81  E-value: 4.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  725 AGSNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPII 804
Cdd:TIGR02154    1 MTRRILVVEDEPAIRELIAYNLEKAGYDVVEAGDGDEALTLINERGPDLILLDWMLPGTSGIELCRRLRRRPETRAIPII 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1237881481  805 AMIANTMLADKNKALDCGMNDYIEKPFNINKLF----SIMRKwITPS 847
Cdd:TIGR02154   81 MLTARGEEEDRVRGLETGADDYITKPFSPRELLarikAVLRR-IRPQ 126
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
729-830 5.29e-10

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


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 57.77  E-value: 5.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:cd17622      3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPK---YQGPILLLTA 79
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17622     80 LDSDIDHILGLELGADDYVVKP 101
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-554 5.36e-10

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: 57.40  E-value: 5.36e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGevivTVMEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAI 527
Cdd:cd16923      1 LQRVFSNLLSNAIKYSPEN----TRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS--RNTEGAGLGLSI 74
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  528 SQKFIELMGGEIWVESEvGKGSEFNIT 554
Cdd:cd16923     75 AKAIIELHGGSASAEYD-DNHDLFKVR 100
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
333-542 5.74e-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: 63.61  E-value: 5.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  333 THFLNN----ISHEIRTPMnAIIGLSHILINS-DLNKKQRQHLDKVHKSAESLLSIINNILDFSNIEAdklTLETSKFKL 407
Cdd:TIGR03785  482 THYLENmssrLSHELRTPV-AVVRSSLENLELqALEQEKQKYLERAREGTERLSMILNNMSEATRLEQ---AIQSAEVED 557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  408 YDLFENLSENLSifAY---DKNIELIFDIPValEDIYI-GDQTKLNQVLLNIVNNAIKFTEYGEVIvtVMEVSRKDTDII 483
Cdd:TIGR03785  558 FDLSEVLSGCMQ--GYqmtYPPQRFELNIPE--TPLVMrGSPELIAQMLDKLVDNAREFSPEDGLI--EVGLSQNKSHAL 631
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  484 LkfNIKDSGAGINLKDIEHVFDAFC--QADGSLTRKHggTGLGLAISQKFIELMGGEIWVE 542
Cdd:TIGR03785  632 L--TVSNEGPPLPEDMGEQLFDSMVsvRDQGAQDQPH--LGLGLYIVRLIADFHQGRIQAE 688
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-548 6.08e-10

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: 57.46  E-value: 6.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEyGEVivtvmEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSltRKHGGTGLGLAI 527
Cdd:cd16950      1 LKRVLSNLVDNALRYGG-GWV-----EVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNA--RGTSGTGLGLAI 72
                           90       100
                   ....*....|....*....|.
gi 1237881481  528 SQKFIELMGGEIWVESEVGKG 548
Cdd:cd16950     73 VQRISDAHGGSLTLANRAGGG 93
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-551 6.33e-10

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: 57.08  E-value: 6.33e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILKFniKDSGAGINLKDIEHVFDAFCQadgslTRKHG-GTGLGLA 526
Cdd:cd16976      1 IQQVLMNLLQNALDAMGKVENPRIRIAARRLGGRLVLVV--RDNGPGIAEEHLSRVFDPFFT-----TKPVGkGTGLGLS 73
                           90       100
                   ....*....|....*....|....*
gi 1237881481  527 ISQKFIELMGGEIWVESEVGKGSEF 551
Cdd:cd16976     74 ISYGIVEEHGGRLSVANEEGAGARF 98
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
729-842 8.98e-10

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 57.12  E-value: 8.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMIA 808
Cdd:cd17550      1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIKE--KYPDLPVIMISG 78
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17550     79 HGTIETAVKATKLGAYDFIEKPLSLDRLLLTIER 112
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
579-689 9.58e-10

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: 57.16  E-value: 9.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseqASRPFELILMDWKMSSDNDFKVLEKIHylvttNNYMRPK 658
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELL----KEERPDLILLDINMPGMDGLELLKRIR-----RRDPTTP 72
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:pfam00072   73 VIILTAHGDEDDAVEALEAGADDFLSKPFDP 103
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
729-830 9.92e-10

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


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 56.68  E-value: 9.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGK--QTPVLMLTA 78
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd19935     79 RDSVEDRVKGLDLGADDYLVKP 100
envZ PRK09467
osmolarity sensor protein; Provisional
339-539 1.01e-09

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 61.85  E-value: 1.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  339 ISHEIRTPmnaiigLSHILINSDLNKKQRQHL-DKVHKSAESLLSIINNILDFsnIEADKltleTSKFKLYDLFENLSEN 417
Cdd:PRK09467   236 VSHDLRTP------LTRIRLATEMMSEEDGYLaESINKDIEECNAIIEQFIDY--LRTGQ----EMPMEMADLNALLGEV 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  418 LSIFA-YDKNIELIFD---IPVALEDIYIgdqtklNQVLLNIVNNAIKFTEyGEVivtvmEVSRKDTDIILKFNIKDSGA 493
Cdd:PRK09467   304 IAAESgYEREIETALQpgpIEVPMNPIAI------KRALANLVVNAARYGN-GWI-----KVSSGTEGKRAWFQVEDDGP 371
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1237881481  494 GINLKDIEHVFDAFCQADGSltRKHGGTGLGLAISQKFIELMGGEI 539
Cdd:PRK09467   372 GIPPEQLKHLFQPFTRGDSA--RGSSGTGLGLAIVKRIVDQHNGKV 415
PRK15479 PRK15479
transcriptional regulator TctD;
729-841 1.14e-09

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 59.73  E-value: 1.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:PRK15479     3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEVLQRLRKRGQ--TLPVLLLTA 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:PRK15479    81 RSAVADRVKGLNVGADDYLPKPFELEELDARLR 113
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
729-830 1.20e-09

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: 56.40  E-value: 1.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVED-NEINSEVTSSLLSlHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSELPIIAMI 807
Cdd:cd17620      1 ILVIEDePQIRRFLRTALEA-HGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDG---LEVIRRLREWSAVPVIVLS 76
                           90       100
                   ....*....|....*....|...
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17620     77 ARDEESDKIAALDAGADDYLTKP 99
PRK10610 PRK10610
chemotaxis protein CheY;
730-837 1.80e-09

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 56.91  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  730 LLVEDNEINSEVTSSLL-SLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:PRK10610     9 LVVDDFSTMRRIVRNLLkELGFNNVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTA 88
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFN-------INKLF 837
Cdd:PRK10610    89 EAKKENIIAAAQAGASGYVVKPFTaatleekLNKIF 124
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
728-842 2.38e-09

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 60.81  E-value: 2.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIrKELNlSELPIIAMI 807
Cdd:PRK10365     7 DILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEI-KALN-PAIPVLIMT 84
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:PRK10365    85 AYSSVETAVEALKTGALDYLIKPLDFDNLQATLEK 119
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-553 2.63e-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: 55.87  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFT--EYGEVIVTV-----MEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFcqadgsLTRKHGG 520
Cdd:cd16918      1 LIQVFLNLVRNAAQALagSGGEIILRTrtqrqVTLGHPRHRLALRVSVIDNGPGIPPDLQDTIFYPM------VSGRENG 74
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  521 TGLGLAISQKFIELMGGEIWVESEVGKgSEFNI 553
Cdd:cd16918     75 TGLGLAIAQNIVSQHGGVIECDSQPGH-TVFSV 106
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
729-842 2.69e-09

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: 56.34  E-value: 2.69e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRkELNlSELPIIAM-- 806
Cdd:cd17549      1 VLLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIR-ELD-PDLPVILItg 78
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1237881481  807 ---IAntmLAdkNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17549     79 hgdVP---MA--VEAMRAGAYDFLEKPFDPERLLDVVRR 112
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
728-840 3.48e-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: 3.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVT-CAINGKDALLKLQRERFDGVLMDCQMP-VMDGYKATQVIRKELNlseLPIIA 805
Cdd:cd17534      2 KILIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD---IPVIF 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKLFSIM 840
Cdd:cd17534     79 LTAYSDEETLERAKETNPYGYLVKPFNERELKAAI 113
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
729-836 5.11e-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: 55.28  E-value: 5.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMIA 808
Cdd:cd17572      1 VLLVEDSPSLAALYQEYLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQE--RSLPTSVIVITA 78
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  809 NtmlADKNKALDC---GMNDYIEKPFNINKL 836
Cdd:cd17572     79 H---GSVDIAVEAmrlGAYDFLEKPFDADRL 106
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
409-554 6.42e-09

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: 55.33  E-value: 6.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  409 DLFENLSENLSIFAYDKNIELIFDIPVALEdiYIGDQTKLNQVLLNIVNNAIKFTEyGEVIVTVMEvsrkdTDIILKFNI 488
Cdd:cd16954      1 PLLDSLCSALNKVYQRKGVSISLDISPELR--FPGERNDLMELLGNLLDNACKWCL-EFVEVTARQ-----TDGGLHLIV 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  489 KDSGAGINLKDIEHVFDAFCQADgsltRKHGGTGLGLAISQKFIELMGGEIWVE-SEVGkGSEFNIT 554
Cdd:cd16954     73 DDDGPGVPESQRSKIFQRGQRLD----EQRPGQGLGLAIAKEIVEQYGGELSLSdSPLG-GARFEVV 134
Hpt pfam01627
Hpt domain; The histidine-containing phosphotransfer (HPt) domain is a novel protein module ...
888-978 1.27e-08

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: 53.12  E-value: 1.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  888 KLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDDGQETDDnlikqvkliDEKI 967
Cdd:pfam01627    1 ELLELFLEEAPELLEQLEQALDAEDLEALFRAAHTLKGSAGSLGLPALAELAHELEDLLREGELPLD---------PELL 71
                           90
                   ....*....|.
gi 1237881481  968 FEVIELISQLD 978
Cdd:pfam01627   72 EALRDLLEALR 82
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
727-804 1.32e-08

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: 53.76  E-value: 1.32e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881481  727 SNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPII 804
Cdd:cd17554      1 KKILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIREK--KPDLPVI 76
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
729-842 1.35e-08

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


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 53.88  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVT---CAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelnlsELPIIA 805
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELGFEvvgEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIRE-----LYPDIK 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1237881481  806 MIantML---ADKN---KALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17536     76 II---ILsgyDDFEyaqKAIRLGVVDYLLKPVDEEELEEALEK 115
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
579-689 1.39e-08

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: 56.12  E-value: 1.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVI--NESMAvkNIITQMLREFGMMVTSAESGYDALSIFSSEqasrPFELILMDWKMSSDNDFKVLEKIHylvttNNYMR 656
Cdd:COG0745      5 LVVedDPDIR--ELLADALEREGYEVDTAADGEEALELLEEE----RPDLILLDLMLPGMDGLEVCRRLR-----ARPSD 73
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  657 PKIILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:COG0745     74 IPIIMLTARDDEEDRVRGLEAGADDYLTKPFDP 106
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
444-539 2.05e-08

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


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 53.23  E-value: 2.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFT-EYGEVIVTVmevsRKDTDIIlKFNIKDSGAGINLKDIEHVFDAFCqadgSLTRKHGG-- 520
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSpEGGLIALQL----EADTEGI-ELLVFDEGSGIPDYALNRVFERFY----SLPRPHSGqk 71
                           90       100
                   ....*....|....*....|
gi 1237881481  521 -TGLGLAISQKFIELMGGEI 539
Cdd:cd16945     72 sTGLGLAFVQEVAQLHGGRI 91
resp_reg_YycF NF040534
response regulator YycF;
729-836 2.18e-08

response regulator YycF;


Pssm-ID: 439744 [Multi-domain]  Cd Length: 231  Bit Score: 55.88  E-value: 2.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELnlsELPIIAMIA 808
Cdd:NF040534     3 ILVVDDEKPIADILEFNLKKEGYEVFCAYDGNEALELVEEEVPDLVLLDIMLPGRDGMEVCREVRKKY---DMPIIMLTA 79
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:NF040534    80 KDSEIDKVLGLELGADDYVTKPFSTREL 107
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
729-841 2.35e-08

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 55.96  E-value: 2.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQrERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLD-DSIDLLLLDVMMPKKNGIDTLKELRQT---HQTPVIMLTA 79
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:PRK10955    80 RGSELDRVLGLELGADDYLPKPFNDRELVARIR 112
PRK10693 PRK10693
two-component system response regulator RssB;
754-860 2.78e-08

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 56.54  E-value: 2.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  754 TCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIANTMLADKNKALDCGMNDYIEKPF-N 832
Cdd:PRK10693     1 VLAANGVDALELLGGFTPDLIICDLAMPRMNGIEFVEHLRNRGD--QTPVLVISATENMADIAKALRLGVQDVLLKPVkD 78
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  833 INKLFSIMRKWITPSkpeIFTSLSEQEN 860
Cdd:PRK10693    79 LNRLREMVFACLYPS---MFNSRVEEEE 103
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
444-550 3.25e-08

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: 52.46  E-value: 3.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADgSLTRKHGGTGL 523
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTV----SISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDD-TSRRSGGHYGM 75
                           90       100
                   ....*....|....*....|....*..
gi 1237881481  524 GLAISQKFIELMGGEIWVESEVGKGSE 550
Cdd:cd16975     76 GLYIAKNLVEKHGGSLIIENSQKGGAE 102
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
729-837 3.35e-08

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: 52.90  E-value: 3.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHK-INV--TCAiNGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIA 805
Cdd:cd17535      1 VLIVDDHPLVREGLRRLLESEPdIEVvgEAA-DGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRR--YPDLKVIV 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKLF 837
Cdd:cd17535     78 LTAHDDPEYVLRALKAGAAGYLLKDSSPEELI 109
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
579-689 4.31e-08

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: 56.90  E-value: 4.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEqasrPFELILMDWKMSSDNDFKVLEKIHylvttNNYMRPK 658
Cdd:COG2204      6 LVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREE----PPDLVLLDLRMPGMDGLELLRELR-----ALDPDLP 76
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:COG2204     77 VILLTGYGDVETAVEAIKAGAFDYLTKPFDL 107
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
448-553 4.42e-08

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


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 52.38  E-value: 4.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVIVTVMEVSRKDTDIILK-----------FNIKDSGAGINLKDIEHVFDAFCQadgslTR 516
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNyrdlipgnyvcLEVSDTGSGMPAEVLRRAFEPFFT-----TK 75
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1237881481  517 KHG-GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:cd16919     76 EVGkGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRI 113
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
750-842 4.71e-08

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


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 52.28  E-value: 4.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  750 KINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELnlSELPIIAMIANTMLADKNKALDCGMNDYIEK 829
Cdd:cd19919     24 GLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLALLAQIKQRH--PDLPVIIMTAHSDLDSAVSAYQGGAFEYLPK 101
                           90
                   ....*....|...
gi 1237881481  830 PFNINKLFSIMRK 842
Cdd:cd19919    102 PFDIDEAVALVER 114
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
729-830 5.05e-08

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: 52.37  E-value: 5.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDG-----------VLMDCQMPVMDGYKATQVIRKELN 797
Cdd:cd17581      1 VLAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALEFLGLEDEEDssnfnepkvnmIITDYCMPGMTGYDLLKKVKESSA 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  798 LSELPIIAMIANTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17581     81 LKEIPVVIMSSENIPTRISRCLEEGAEDFLLKP 113
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
728-842 5.15e-08

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: 52.28  E-value: 5.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLH-KINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKEL-NLSELPIIA 805
Cdd:cd17542      2 KVLIVDDAAFMRMMLKDILTKAgYEVVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIKKIDpNAKVIMCSA 81
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1237881481  806 MIANTMLADKNKAldcGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17542     82 MGQEEMVKEAIKA---GAKDFIVKPFQPERVLEAVEK 115
HATPase_Phy-like cd16932
Histidine kinase-like ATPase domain of plant phytochromes similar to Arabidopsis thaliana ...
443-557 5.70e-08

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: 51.89  E-value: 5.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  443 GDQTKLNQVLLNIVNNAIKFTEYGEVIVTVmEVSRKDTDII-------LKFNIKDSGAGINLKDIEHVFDAfcqaDGSLT 515
Cdd:cd16932      2 GDQIRLQQVLADFLLNAVRFTPSPGGWVEI-KVSPTKKQIGdgvhvihLEFRITHPGQGLPEELVQEMFEE----NQWTT 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1237881481  516 RKhggtGLGLAISQKFIELMGGEIWVESEVGKgSEFNITTQL 557
Cdd:cd16932     77 QE----GLGLSISRKLVKLMNGDVRYLREAGR-SYFLITLEL 113
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
751-836 5.73e-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: 52.15  E-value: 5.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  751 INVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMIANTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17593     26 VEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVE--QLETKVIVVSGDVQPEAKERVLELGALAFLKKP 103

                   ....*.
gi 1237881481  831 FNINKL 836
Cdd:cd17593    104 FDPEKL 109
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
579-699 6.20e-08

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: 53.81  E-value: 6.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMV-TSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKIhylvtTNNYMRP 657
Cdd:COG3707      7 LVVDDEPLRRADLREGLREAGYEVvAEAADGEDAVELVRELK----PDLVIVDIDMPDRDGLEAARQI-----SEERPAP 77
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1237881481  658 kIILVTDYGQEEFDLVTNDLGVDAFVNKPVTPYNMAKSLLIA 699
Cdd:COG3707     78 -VILLTAYSDPELIERALEAGVSAYLVKPLDPEDLLPALELA 118
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
444-554 6.56e-08

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


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 51.77  E-value: 6.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  444 DQTKLNQVLLNIVNNA---IKFTEYGEVIVTVMEVSRKDTDIILkfNIKDSGAGINLKDIEHVFDAFcqadgsLTRKHGG 520
Cdd:cd16944      1 DTTQISQVLTNILKNAaeaIEGRPSDVGEVRIRVEADQDGRIVL--IVCDNGKGFPREMRHRATEPY------VTTRPKG 72
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  521 TGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16944     73 TGLGLAIVKKIMEEHGGRISLSNREAGGACIRII 106
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
728-808 7.53e-08

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


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 52.20  E-value: 7.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLH-KINV-TCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIrkelnLS--ELPI 803
Cdd:COG2197      3 RVLIVDDHPLVREGLRALLEAEpDIEVvGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL-----LTprEREV 77

                   ....*
gi 1237881481  804 IAMIA 808
Cdd:COG2197     78 LRLLA 82
pleD PRK09581
response regulator PleD; Reviewed
729-838 1.01e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 55.68  E-value: 1.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:PRK09581     5 ILVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTA 84
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFS 838
Cdd:PRK09581    85 LDDPEDRVRGLEAGADDFLTKPINDVALFA 114
HATPase_ETR2_ERS2-EIN4-like cd16938
Histidine kinase-like ATPase domain of Arabidopsis thaliana ETR2, ERS2, and EIN4, and related ...
437-554 1.12e-07

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


Pssm-ID: 340415 [Multi-domain]  Cd Length: 133  Bit Score: 51.69  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  437 LEDIYIGDQTKLNQVLLNIVNNAIKFTE-YGEVIVTV------MEVSRKDTDIILKFNIKDSGA---GINLKDIEHVFDA 506
Cdd:cd16938      1 LPDVVVGDERRVFQVLLHMLGNLLKMRNgGGNITFRVfleggsEDRSDRDWGPWRPSMSDESVEirfEVEINDSGSPSIE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1237881481  507 FCQADGSLTRKHG----GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNIT 554
Cdd:cd16938     81 SASMRNSLNRRYNlselGEHLSFSICKQLVQLMGGNIWIVPGSGLGTTMSLL 132
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
579-696 1.14e-07

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: 51.25  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEQASrpFELILMDWKMSSDNDFKVLEKIHYLVTtnNYMRPK 658
Cdd:cd19933      4 LLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHS--FQLVLLDLCMPEMDGFEVALRIRKLFG--RRERPL 79
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPVTPYNMAKSL 696
Cdd:cd19933     80 IVALTANTDDSTREKCLSLGMNGVITKPVSLHALGDEL 117
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
727-857 1.21e-07

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 53.65  E-value: 1.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVED-NEINSEVTSSLLSlHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSELPIIA 805
Cdd:PRK10529     2 TNVLIVEDeQAIRRFLRTALEG-DGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDG---IEFIRDLRQWSAIPVIV 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKLFS----IMRKWITPSKPEIFTSLSE 857
Cdd:PRK10529    78 LSARSEESDKIAALDAGADDYLSKPFGIGELQArlrvALRRHSATPAPDPLVKFSD 133
pleD PRK09581
response regulator PleD; Reviewed
602-837 1.37e-07

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 55.29  E-value: 1.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  602 VTSAESGYDALSIFSSEQAsrpfELILMDWKMSSDNDFKVLEKIHYLVTTNNYmrPkIILVTDYGQEEfDLVTN-DLGVD 680
Cdd:PRK09581    29 VLTASSGAEAIAICEREQP----DIILLDVMMPGMDGFEVCRRLKSDPATTHI--P-VVMVTALDDPE-DRVRGlEAGAD 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  681 AFVNKPVTPYNM---AKSLL---IAFNE-SLNDITHHLPETNNLNNMTKLLAGSN--ILLVEDNEINSE-VTSSLLSLHK 750
Cdd:PRK09581   101 DFLTKPINDVALfarVKSLTrlkMVIDElRLRASTNAEIGVTALMIMAYANKDEDgrILLVDDDVSQAErIANILKEEFR 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  751 inVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMI---ANTMLAdknKALDCGMNDYI 827
Cdd:PRK09581   181 --VVVVSDPSEALFNAAETNYDLVIVSANFENYDPLRLCSQLRSKERTRYVPILLLVdedDDPRLV---KALELGVNDYL 255
                          250
                   ....*....|
gi 1237881481  828 EKPFNINKLF 837
Cdd:PRK09581   256 MRPIDKNELL 265
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
729-830 2.02e-07

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: 50.23  E-value: 2.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnLSELPIIAMIA 808
Cdd:cd19926      1 VLVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHIQQR--LPQTPVAVITA 78
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd19926     79 YGSLDTAIEALKAGAFDFLTKP 100
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
579-686 2.66e-07

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: 49.77  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMM--VTSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKIHylvttNNYMR 656
Cdd:COG4753      3 LIVDDEPLIREGLKRILEWEAGFevVGEAENGEEALELLEEHK----PDLVITDINMPGMDGLELLEAIR-----ELDPD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  657 PKIILVTDYGQEEFDLVTNDLGVDAFVNKP 686
Cdd:COG4753     74 TKIIILSGYSDFEYAQEAIKLGADDYLLKP 103
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
729-840 2.80e-07

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


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 50.10  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTC-AINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMi 807
Cdd:cd19932      3 VLIAEDEALIRMDLREMLEEAGYEVVGeASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE---NIAPIVLL- 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  808 anTMLADKN---KALDCGMNDYIEKPFNINKLFSIM 840
Cdd:cd19932     79 --TAYSQQDlveRAKEAGAMAYLVKPFSESDLIPAI 112
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
729-831 4.12e-07

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


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 49.68  E-value: 4.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelnLSELPIIAMIA 808
Cdd:cd19938      2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRR---FSDVPIIMVTA 78
                           90       100
                   ....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd19938     79 RVEEIDRLLGLELGADDYICKPY 101
ompR PRK09468
osmolarity response regulator; Provisional
726-836 4.20e-07

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 52.28  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  726 GSNILLVEDNEINSEVTSSLLSLHKINVTCAINGK--DALLklQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPI 803
Cdd:PRK09468     5 NYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEqmDRLL--TRESFHLMVLDLMLPGEDGLSICRRLRSQNN--PTPI 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  804 IAMIANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:PRK09468    81 IMLTAKGEEVDRIVGLEIGADDYLPKPFNPREL 113
glnL PRK11073
nitrogen regulation protein NR(II);
426-553 5.32e-07

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 53.16  E-value: 5.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  426 NIELIFDIPVALEDIYIgDQTKLNQVLLNIVNNAIKF--TEYGEVIV---TVMEVS--RKDTDIILKFNIKDSGAGI--N 496
Cdd:PRK11073   217 NVRLIRDYDPSLPELAH-DPDQIEQVLLNIVRNALQAlgPEGGTITLrtrTAFQLTlhGERYRLAARIDIEDNGPGIppH 295
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  497 LKDIehVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKgSEFNI 553
Cdd:PRK11073   296 LQDT--LFYPM------VSGREGGTGLGLSIARNLIDQHSGKIEFTSWPGH-TEFSV 343
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
421-553 9.79e-07

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 52.61  E-value: 9.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  421 FAYDKNIELIFDIPVALEDIYIGDQT-KLNQVLLNIVNN---AIKFTEYGEVivtvmEVSRKDTDIILKFNIKDSGAGIN 496
Cdd:PRK11086   406 RARELGITLIISEDSQLPDSGDEDQVhELITILGNLIENaleAVGGEEGGEI-----SVSLHYRNGWLHCEVSDDGPGIA 480
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  497 LKDIEHVFDafcqaDGSLTrKHGGTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:PRK11086   481 PDEIDAIFD-----KGYST-KGSNRGVGLYLVKQSVENLGGSIAVESEPGVGTQFFV 531
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
448-542 9.91e-07

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: 48.34  E-value: 9.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  448 LNQVLLNIVNNAIKFTEYGEVIVTVmevSRKDTDIILKFNIKDSGAGINLKDIEHVFDAFCQADGSLTRKHGGTGLGLAI 527
Cdd:cd16953      1 LGQVLRNLIGNAISFSPPDTGRITV---SAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYTERPANEAFGQHSGLGLSI 77
                           90
                   ....*....|....*
gi 1237881481  528 SQKFIELMGGEIWVE 542
Cdd:cd16953     78 SRQIIEAHGGISVAE 92
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
729-836 1.62e-06

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: 47.79  E-value: 1.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKatqvIRKELNLSEL--PIIAM 806
Cdd:cd17616      1 VLLIEDDSATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYE----VLRTLRLAKVktPILIL 76
                           90       100       110
                   ....*....|....*....|....*....|
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17616     77 SGLADIEDKVKGLGFGADDYMTKPFHKDEL 106
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
729-830 2.35e-06

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: 47.05  E-value: 2.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPIIAMIA 808
Cdd:cd19936      1 IALVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLRQK---STLPVIFLTS 77
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd19936     78 KDDEIDEVFGLRMGADDYITKP 99
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
729-830 2.71e-06

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: 47.01  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDA--LLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAM 806
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAwdVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIMM 80
                           90       100
                   ....*....|....*....|....
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17582     81 SSQDSVGVVFKCLSKGAADYLVKP 104
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
728-857 5.15e-06

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 50.25  E-value: 5.15e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLseLPIIAMI 807
Cdd:PRK10923     5 IVWVVDDDSSIRWVLERALAGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDGLALLKQIKQRHPM--LPVIIMT 82
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWIT-------PSKPEIFTSLSE 857
Cdd:PRK10923    83 AHSDLDAAVSAYQQGAFDYLPKPFDIDEAVALVERAIShyqeqqqPRNIQVNGPTTD 139
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
323-552 5.22e-06

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


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 50.46  E-value: 5.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  323 IQAEK-ANETKThfLNNISHEIRTPMNAIIGLSHILINSDLNKKQRQ---HLDKVHKSAESLLSIINNILDFSNIEADKL 398
Cdd:COG4192    425 IQAAKmAVVGQT--MTSLAHELNQPLNAMSMYLFSAKKALEQENYAQlptSLDKIEGLIERMDKIIKSLRQFSRKSDTPL 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  399 TLetskFKLYDLFENLSENLSIFAYDKNIELIF--DIPValediyIGDQTKLNQVLLNIVNNAIKFTEYGEVIVtvmeVS 476
Cdd:COG4192    503 QP----VDLRQVIEQAWELVESRAKPQQITLHIpdDLMV------QGDQVLLEQVLVNLLVNALDAVATQPQIS----VD 568
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  477 RKDTDIILKFNIKDSGAGINLkdIEHVFDAFcqadgsLTRKHGGTGLGLAISQKFIELMGGEIWVESEVGKGS----EFN 552
Cdd:COG4192    569 LLSNAENLRVAISDNGNGWPL--VDKLFTPF------TTTKEVGLGLGLSICRSIMQQFGGDLYLASTLERGAmvilEFN 640
PRK10643 PRK10643
two-component system response regulator PmrA;
729-844 5.71e-06

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 48.49  E-value: 5.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:PRK10643     3 ILIVEDDTLLLQGLILALQTEGYACDCASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKY--TLPVLILTA 80
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWI 844
Cdd:PRK10643    81 RDTLEDRVAGLDVGADDYLVKPFALEELHARIRALI 116
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
729-796 5.86e-06

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: 46.50  E-value: 5.86e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHK-IN-VTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKEL 796
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEDdLEvVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELREEL 70
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
729-830 7.13e-06

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


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 45.82  E-value: 7.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17602      1 VACVDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTG 80
                           90       100
                   ....*....|....*....|..
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKP 830
Cdd:cd17602     81 KDGLVDRIRAKMAGASGYLTKP 102
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
729-868 8.32e-06

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 48.18  E-value: 8.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVMLTA 84
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEIFTSLSEQENINLSHNSN 868
Cdd:PRK10161    85 RGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAVEEVIEMQGLSLDPTSH 144
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
729-831 1.15e-05

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: 45.19  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRER-FDGVLMDCQMPVMDGYKATQVIRKeLNlSELPIIAMI 807
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGKdIDIVVTDIVMPEMDGIELAREARK-ID-PDVKILFIS 79
                           90       100
                   ....*....|....*....|....
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd18160     80 GGAAAAPELLSDAVGDNATLKKPF 103
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
753-831 1.16e-05

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 48.61  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  753 VTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIrkeLNLSELPIIaMI--------ANTMladknKALDCGMN 824
Cdd:PRK00742    32 VGTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDALEKI---MRLRPTPVV-MVssltergaEITL-----RALELGAV 102

                   ....*..
gi 1237881481  825 DYIEKPF 831
Cdd:PRK00742   103 DFVTKPF 109
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
728-831 1.39e-05

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 47.65  E-value: 1.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAMI 807
Cdd:PRK11083     5 TILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLLA--FHPALPVIFLT 82
                           90       100
                   ....*....|....*....|....
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPF 831
Cdd:PRK11083    83 ARSDEVDRLVGLEIGADDYVAKPF 106
PRK15115 PRK15115
response regulator GlrR; Provisional
727-849 1.49e-05

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 48.68  E-value: 1.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelNLSELPIIAM 806
Cdd:PRK15115     6 AHLLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMQLFAEIQK--VQPGMPVIIL 83
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKP 849
Cdd:PRK15115    84 TAHGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDALEQSAP 126
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
728-870 1.50e-05

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


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 47.50  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHK-IN-VTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSELPIIA 805
Cdd:COG3279      3 KILIVDDEPLARERLERLLEKYPdLEvVGEASNGEEALELLEEHKPDLVFLDIQMPGLDG---FELARQLRELDPPPPII 79
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1237881481  806 MIanTmlADKNKALDcGMN----DYIEKPFNINKLFSIMRKWI--TPSKPEIFTSLSEQENINLSHNSNII 870
Cdd:COG3279     80 FT--T--AYDEYALE-AFEvnavDYLLKPIDEERLAKALEKAKerLEAKAAAEASPEEKDRIFVKSGGKLV 145
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
576-689 1.56e-05

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: 45.41  E-value: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  576 INTLVINESMAVKNIITQMLREFGMM-VTSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKIHylvTTNNY 654
Cdd:cd19923      1 MKVLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGG----FDFVITDWNMPNMDGLELLKTIR---ADGAL 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  655 MRPKIILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:cd19923     74 SHLPVLMVTAEAKKENVIAAAQAGVNNYIVKPFTA 108
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
727-891 1.89e-05

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: 46.45  E-value: 1.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  727 SNILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYkatQVIRKelnLSEL----P 802
Cdd:COG4567      5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGL---DLIEA---LRERdpdaR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  803 II-----AMIANTMLADKNKALdcgmnDYIEKPFNINKLFSIMRKWI--TPSKPEIFTSLS--EQENInlshnsniinfQ 873
Cdd:COG4567     79 IVvltgyASIATAVEAIKLGAD-----DYLAKPADADDLLAALERAEgdAPAPPENPMSLDrlEWEHI-----------Q 142
                          170
                   ....*....|....*...
gi 1237881481  874 VGLEICSGSVSLYQKLLK 891
Cdd:COG4567    143 RVLAECDGNISATARALG 160
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
729-842 3.20e-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: 44.12  E-value: 3.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykatQVIRKELNL--SELPIIAM 806
Cdd:cd17537      3 VYVVDDDEAVRDSLAFLLRSVGLAVKTFTSASAFLAAAPPDQPGCLVLDVRMPGMSG----LELQDELLArgSNIPIIFI 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  807 IANTMLADKNKALDCGMNDYIEKPFNINKLFSIMRK 842
Cdd:cd17537     79 TGHGDVPMAVEAMKAGAVDFLEKPFRDQVLLDAIEQ 114
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
728-836 3.46e-05

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 44.16  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAI--NGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIA 805
Cdd:cd19925      2 NVLIVEDDPMVAEIHRAYVEQVPGFTVIGTagTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELRAAGH--DVDVIV 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd19925     80 VTAANDVETVREALRLGVVDYLIKPFTFERL 110
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
757-831 4.11e-05

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 46.22  E-value: 4.11e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1237881481  757 INGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelnLSELPIIAMIANTMLADKNKALDCGMNDYIEKPF 831
Cdd:PRK10710    41 SHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIRR---FSDIPIVMVTAKIEEIDRLLGLEIGADDYICKPY 112
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
574-696 4.80e-05

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


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 44.19  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  574 KNINTLVINESMAVKNIITQMLREFG--MMVTSAESGYDALSIFsseqASRPFELILMDWKMSSDNDFKVLEKIHylvtt 651
Cdd:COG4565      2 KMIRVLIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALL----AEHRPDLILLDIYLPDGDGLELLRELR----- 72
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1237881481  652 NNYMRPKIILVTDYGQEEFDLVTNDLGVDAFVNKPVTPYNMAKSL 696
Cdd:COG4565     73 ARGPDVDVIVITAARDPETVREALRAGVVDYLIKPFTFERLREAL 117
PRK10610 PRK10610
chemotaxis protein CheY;
574-696 5.90e-05

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 43.81  E-value: 5.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  574 KNINTLVINESMAVKNIITQMLREFGMM-VTSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKIHylvTTN 652
Cdd:PRK10610     4 KELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGG----FGFVISDWNMPNMDGLELLKTIR---ADG 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1237881481  653 NYMRPKIILVTDYGQEEFDLVTNDLGVDAFVNKPVTPYNMAKSL 696
Cdd:PRK10610    77 AMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
589-686 7.93e-05

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: 42.78  E-value: 7.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  589 NIITQMLREFGMMVTSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKIhylvtTNNYMRPKIILVTDYGQE 668
Cdd:cd17574     11 ELLSDYLEKEGYEVDTAADGEEALELAREEQ----PDLIILDVMLPGMDGFEVCRRL-----REKGSDIPIIMLTAKDEE 81
                           90
                   ....*....|....*....
gi 1237881481  669 EfDLVTN-DLGVDAFVNKP 686
Cdd:cd17574     82 E-DKVLGlELGADDYITKP 99
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
728-830 1.06e-04

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 45.64  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSL---HKInVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKElnlSELPII 804
Cdd:PRK12555     2 RIGIVNDSPLAVEALRRALARdpdHEV-VWVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRRIMAE---RPCPIL 77
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  805 aMIanTMLADKN-----KALDCGMNDYIEKP 830
Cdd:PRK12555    78 -IV--TSLTERNasrvfEAMGAGALDAVDTP 105
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
579-687 1.12e-04

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 42.82  E-value: 1.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDalsiFSSEQASRPFELILMDWKMSSDNDFKVLEKIHYLVTTnnymrPK 658
Cdd:cd17594      3 LVVDDDAAMRHLLILYLRERGFDVTAAADGAE----EARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV-----PI 73
                           90       100
                   ....*....|....*....|....*....
gi 1237881481  659 IILVTDYGQEEFDLVTNDLGVDAFVNKPV 687
Cdd:cd17594     74 IIISGDRRDEIDRVVGLELGADDYLAKPF 102
PRK10336 PRK10336
two-component system response regulator QseB;
729-831 1.51e-04

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 44.50  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRkELNLSElPIIAMIA 808
Cdd:PRK10336     3 ILLIEDDMLIGDGIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWR-EKGQRE-PVLILTA 80
                           90       100
                   ....*....|....*....|...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPF 831
Cdd:PRK10336    81 RDALAERVEGLRLGADDYLCKPF 103
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
579-633 1.68e-04

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: 40.24  E-value: 1.68e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 1237881481   579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEQasrpFELILMDWKM 633
Cdd:smart00448    4 LVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEK----PDLILLDIMM 54
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
728-831 1.83e-04

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: 41.83  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDN-EINSEVTSSLLSLHKINVT-CAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIA 805
Cdd:cd17561      3 KVLIADDNrEFVQLLEEYLNSQPDMEVVgVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIM 82
                           90       100
                   ....*....|....*....|....*.
gi 1237881481  806 MIANTMLADKNKALDCGMNDYIEKPF 831
Cdd:cd17561     83 LTAFGQEDITQRAVELGASYYILKPF 108
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
756-844 1.93e-04

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 42.16  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  756 AINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIrKELNlSELPIIAMIANTMLADKNKALDCGMNDYIEKPFNINK 835
Cdd:cd17553     30 AANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRM-KVID-ENIRVIIMTAYGELDMIQESKELGALTHFAKPFDIDE 107

                   ....*....
gi 1237881481  836 LFSIMRKWI 844
Cdd:cd17553    108 IRDAVKKYL 116
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
728-785 2.85e-04

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


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 41.27  E-value: 2.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDG 785
Cdd:cd17563      2 SLLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSG 59
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
728-842 2.88e-04

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: 41.62  E-value: 2.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNLSelPIIAMI 807
Cdd:cd17569      2 TILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDG---AELLKRVRERY--PDTVRI 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1237881481  808 ANTMLADKNKALDCgMND-----YIEKPFNINKLFSIMRK 842
Cdd:cd17569     77 LLTGYADLDAAIEA-INEgeiyrFLTKPWDDEELKETIRQ 115
PRK13856 PRK13856
two-component response regulator VirG; Provisional
728-841 3.53e-04

two-component response regulator VirG; Provisional


Pssm-ID: 172377 [Multi-domain]  Cd Length: 241  Bit Score: 43.26  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYkatQVIRKELNLSELPIIaMI 807
Cdd:PRK13856     3 HVLVIDDDVAMRHLIVEYLTIHAFKVTAVADSQQFNRVLASETVDVVVVDLNLGREDGL---EIVRSLATKSDVPII-II 78
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1237881481  808 ANTML--ADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:PRK13856    79 SGDRLeeADKVVALELGATDFIAKPFGTREFLARIR 114
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
579-645 3.62e-04

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: 41.03  E-value: 3.62e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEQasrpFELILMDWKMSSDNDFKVLEKI 645
Cdd:cd17555      4 LVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQ----PDLVLCDLRMPEMDGLEVLKQI 66
HPT cd00088
Histidine Phosphotransfer domain, involved in signalling through a two part component systems ...
899-978 5.33e-04

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


Pssm-ID: 238041 [Multi-domain]  Cd Length: 94  Bit Score: 40.06  E-value: 5.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  899 DFLQRFENLILE----KNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFDdgqETDDNLIKQVKLIDEKIFEVIELI 974
Cdd:cd00088     14 ELLEELERALLEledaEDLNEIFRAAHTLKGSAASLGLQRLAQLAHQLEDLLD---ALRDGLEVTPELIDLLLDALDALK 90

                   ....
gi 1237881481  975 SQLD 978
Cdd:cd00088     91 AELE 94
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
719-830 6.10e-04

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: 40.33  E-value: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  719 NMTKLLAGsnilLVEDNEINSEVTSsllslhkinvtcAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKELNL 798
Cdd:cd17565      9 NIIKILSD----IIEDDDLGEVVGE------------ADNGAQAYDEILFLQPDIVLIDLLMPGMDG---IQLVRKLKDT 69
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  799 SELPIIAMIANTMLAD-KNKALDCGMNDYIEKP 830
Cdd:cd17565     70 GSNGKFIMISQVSDKEmIGKAYQAGIEFFINKP 102
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
579-689 6.19e-04

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: 40.52  E-value: 6.19e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseqASRPFELILMDWKMSSDNDFKVLEKIHYLVttnNYMRPK 658
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAA----QRFRPDVILSDIGMPGMDGYELARRLRELP---WLANTP 74
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1237881481  659 IILVTDYGQEEfdlvtnDL------GVDAFVNKPVTP 689
Cdd:cd17580     75 AIALTGYGQPE------DReraleaGFDAHLVKPVDP 105
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
579-686 6.32e-04

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: 40.18  E-value: 6.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEQasrPFELILMDWKMSSDNDF---KVLEKIHYLVttnnym 655
Cdd:cd18160      3 LLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQGK---DIDIVVTDIVMPEMDGIelaREARKIDPDV------ 73
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1237881481  656 rpKIILVTDYGQEEFDLVTNDLGVDAFVNKP 686
Cdd:cd18160     74 --KILFISGGAAAAPELLSDAVGDNATLKKP 102
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
729-836 7.37e-04

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


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 42.01  E-value: 7.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIR--KELNlSELPIIAM 806
Cdd:COG4566      2 VYIVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSG---LELQEelAARG-SPLPVIFL 77
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  807 -----IANTMLADKNKALdcgmnDYIEKPFNINKL 836
Cdd:COG4566     78 tghgdVPMAVRAMKAGAV-----DFLEKPFDDQAL 107
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
729-838 7.51e-04

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 40.32  E-value: 7.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDN-EINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPV-MDGYKATQVIRKELNLSELPIIAM 806
Cdd:cd17589      1 FLIVDDQpTFRSMLKSMLRSLGVTRIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPSTVFIM 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1237881481  807 I-ANTMLADKNKALDCGMNDYIEKPFNINKLFS 838
Cdd:cd17589     81 VtGESSRAMVLSALELEPDDYLLKPFTVSELRE 113
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
729-844 1.23e-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: 39.99  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSE-VTSSLLSLHKinVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLSELPIIami 807
Cdd:cd17539      1 VLLVDDRPSSAErIAAMLSSEHE--VVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPIL--- 75
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1237881481  808 antMLADKN------KALDCGMNDYIEKPFNINKLFSIMRKWI 844
Cdd:cd17539     76 ---AVADPGdrgrliRALEIGVNDYLVRPIDPNELLARVRTQI 115
PRK10816 PRK10816
two-component system response regulator PhoP;
729-841 1.40e-03

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 41.26  E-value: 1.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRK-ELNLSELPIIAMI 807
Cdd:PRK10816     3 VLVVEDNALLRHHLKVQLQDAGHQVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDG---LSLIRRwRSNDVSLPILVLT 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFNINKLFSIMR 841
Cdd:PRK10816    80 ARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQ 113
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
729-836 1.44e-03

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


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 39.34  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPvmDGYKATQVIRKELNLSELPIIAMIA 808
Cdd:cd17573      1 ILLIEDDSTLGKEISKGLNEKGYQADVAESLKDGEYYIDIRNYDLVLVSDKLP--DGNGLSIVSRIKEKHPSIVVIVLSD 78
                           90       100
                   ....*....|....*....|....*...
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKL 836
Cdd:cd17573     79 NPKTEQEIEAFKEGADDYIAKPFDFKVL 106
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
425-546 1.65e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 42.31  E-value: 1.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  425 KNIELIFDIPValEDIYIGDQTKLNQVLLNIVNNAIKFT-EYgevivtvMEVSRKDTDIILKFNIKDSGAGINLKDIEHV 503
Cdd:PRK10815   358 KGVNITLDISP--EITFVGEKNDFMEVMGNVLDNACKYClEF-------VEISARQTDEHLHIVVEDDGPGIPESKRELI 428
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1237881481  504 FDAFCQADgsltRKHGGTGLGLAISQKFIELMGGEIWV-ESEVG 546
Cdd:PRK10815   429 FDRGQRAD----TLRPGQGLGLSVAREITEQYEGKISAgDSPLG 468
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
729-854 2.07e-03

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 41.06  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNlsELPIIAMIA 808
Cdd:PRK09836     3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANK--GMPILLLTA 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1237881481  809 NTMLADKNKALDCGMNDYIEKPFNINKLFSIMRKWITPSKPEIFTS 854
Cdd:PRK09836    81 LGTIEHRVKGLELGADDYLVKPFAFAELLARVRTLLRRGAAVIIES 126
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
579-689 2.41e-03

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 40.86  E-value: 2.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESgYDAlsifSSEQASRPF-ELILMDWKMSSDNDFKVLEKIHYLVTTNNYmrp 657
Cdd:PRK10161     6 LVVEDEAPIREMVCFVLEQNGFQPVEAED-YDS----AVNQLNEPWpDLILLDWMLPGGSGIQFIKHLKRESMTRDI--- 77
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1237881481  658 KIILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:PRK10161    78 PVVMLTARGEEEDRVRGLETGADDYITKPFSP 109
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
335-542 2.54e-03

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 41.49  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  335 FLNNISHEIRTPmnaiigLSHILINSDLNKKQR--------QHLDKVHKSAESLLSIINNILDFSNIEADKLTLetskfk 406
Cdd:PRK10755   140 FTADVAHELRTP------LAGIRLHLELLEKQHhidvapliARLDQMMHTVEQLLQLARAGQSFSSGHYQTVKL------ 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  407 LYDLFENLSENLSIFAYDKNIELifDIPVALEDIYI-GDQTKLNQVLLNIVNNAIKFTEYGEVIvtvmEVSRKDTDIILK 485
Cdd:PRK10755   208 LEDVILPSQDELSEMLEQRQQTL--LLPESAADITVqGDATLLRLLLRNLVENAHRYSPEGSTI----TIKLSQEDGGAV 281
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1237881481  486 FNIKDSGAGINLKDIEHVFDAFCQADgsltRKHGGTGLGLAISQKFIELMGGEIWVE 542
Cdd:PRK10755   282 LAVEDEGPGIDESKCGELSKAFVRMD----SRYGGIGLGLSIVSRITQLHHGQFFLQ 334
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
756-842 2.54e-03

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: 38.67  E-value: 2.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  756 AINGKDALLKLQRERFDGVLMDCQMPVMDGYkatQVIRKELNLSELPIIAMIAntmlADKN---KALDCGMNDYIEKPFN 832
Cdd:cd17532     30 AENGEEALEAIEELKPDVVFLDIQMPGLDGL---ELAKKLSKLAKPPLIVFVT----AYDEyavEAFELNAVDYLLKPFS 102
                           90
                   ....*....|
gi 1237881481  833 INKLFSIMRK 842
Cdd:cd17532    103 EERLAEALAK 112
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
576-689 2.74e-03

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: 38.80  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  576 INTLVINESMAVKNIITQMLREFGM-MVTSAESGYDALSIFsseQASRPfELILMDWKMSSDNDFKVLEKIhyLVTTNNy 654
Cdd:cd17542      1 KKVLIVDDAAFMRMMLKDILTKAGYeVVGEAANGEEAVEKY---KELKP-DLVTMDITMPEMDGIEALKEI--KKIDPN- 73
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1237881481  655 mrPKIILVTDYGQEEFDLVTNDLGVDAFVNKPVTP 689
Cdd:cd17542     74 --AKVIMCSAMGQEEMVKEAIKAGAKDFIVKPFQP 106
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
577-689 2.77e-03

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: 38.77  E-value: 2.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  577 NTLVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFsseqASRPFELILMDWKMSsdnDFKVLEKIHYLVTTNNYMR 656
Cdd:cd17618      2 TILIVEDEPAIREMIAFNLERAGFDVVEAEDAESAVNLI----VEPRPDLILLDWMLP---GGSGIQFIRRLKRDEMTRD 74
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1237881481  657 PKIILVTDYGqEEFDLVTN-DLGVDAFVNKPVTP 689
Cdd:cd17618     75 IPIIMLTARG-EEEDKVRGlEAGADDYITKPFSP 107
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
579-689 3.06e-03

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: 38.41  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSSEqasrPFELILMDWKMSSDNDFKVLEKIHylvTTNNYMRPK 658
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDE----KPDLIILDLMLPGIDGLEVCRILR---SDPKTSSIP 73
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1237881481  659 IILVTDYGqEEFDLVTN-DLGVDAFVNKPVTP 689
Cdd:cd19937     74 IIMLTAKG-EEFDKVLGlELGADDYITKPFSP 104
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
579-693 3.34e-03

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: 38.38  E-value: 3.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  579 LVINESMAVKNIITQMLREFGMMVTSAESGYDALSIFSsEQASRpFELILMDWKMSSDNDFKVLEKIHylvttnNYMRPK 658
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLR-ENKDE-FDLVITDVHMPDMDGFEFLELIR------LEMDLP 73
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1237881481  659 IILVTDYGQEE--FDLVTNdlGVDAFVNKPVTPYNMA 693
Cdd:cd17584     74 VIMMSADGSTStvMKGLAH--GACDYLLKPVSIEDLK 108
HPT smart00073
Histidine Phosphotransfer domain; Contains an active histidine residue that mediates ...
884-947 3.36e-03

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


Pssm-ID: 197502 [Multi-domain]  Cd Length: 92  Bit Score: 38.00  E-value: 3.36e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1237881481   884 SLYQKLLKKFADSECDFLQRFENLILEKNRSAAKRQAHSLRGVSGNIGAANINNLAEQLERSFD 947
Cdd:smart00073    4 ELFREELAEFLQSLEEGLLELEKALDAQDVNEIFRAAHTLKGSAGSLGLQQLAQLCHQLENLLD 67
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
728-836 3.71e-03

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


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 38.58  E-value: 3.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLS-LHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGykaTQVIRKeLNLSELPIIAM 806
Cdd:cd17530      2 RVLVLDDDPFQCMMAATILEdLGPGNVDEADDGREALVILLCNAPDIIICDLKMPDMDG---IEFLRH-LAESHSNAAVI 77
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1237881481  807 IANTM-----LADKNKALDCGMN--DYIEKPFNINKL 836
Cdd:cd17530     78 LMSGLdggilESAETLAGANGLNllGTLSKPFSPEEL 114
HATPase_PDK-like cd16929
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ...
407-548 3.86e-03

Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.


Pssm-ID: 340406 [Multi-domain]  Cd Length: 169  Bit Score: 39.25  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  407 LYDLFENLSENLSIFAYDKNI---ELIFDIPVALEDIYIgdQTKLNQVLLNIVNNAIKFT-EYGEVIVTVME-----VSR 477
Cdd:cd16929      2 PKKVVEDASEEARVLCDDYYLsspELEIEGDPSIRFPYV--PSHLYYILFELLKNAMRATvESHGDDSDDLPpikvtVAK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  478 KDTDIILKfnIKDSGAGINLKDIEHVF------------DAFCQADGSLTRKH-GGTGLGLAISQKFIELMGGEIWVESE 544
Cdd:cd16929     80 GDEDLTIK--ISDRGGGIPREDLARLFsymystapqpslDDFSDLISGTQPSPlAGFGYGLPMSRLYAEYFGGDLDLQSM 157

                   ....
gi 1237881481  545 VGKG 548
Cdd:cd16929    158 EGYG 161
PRK11173 PRK11173
two-component response regulator; Provisional
728-832 6.50e-03

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 39.61  E-value: 6.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  728 NILLVEDNEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKELNLselPIIAMI 807
Cdd:PRK11173     5 HILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANV---ALMFLT 81
                           90       100
                   ....*....|....*....|....*
gi 1237881481  808 ANTMLADKNKALDCGMNDYIEKPFN 832
Cdd:PRK11173    82 GRDNEVDKILGLEIGADDYITKPFN 106
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
520-553 7.24e-03

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


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 38.72  E-value: 7.24e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1237881481  520 GTGLGLAISQKFIELMGGEIWVESEVGKGSEFNI 553
Cdd:cd16916    142 GRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTI 175
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
729-841 7.34e-03

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 37.73  E-value: 7.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1237881481  729 ILLVEDnEINSEVTSSLLSLHKINVTCAINGKDALLKLQRERFDGVLMDCQMPVMDGYKATQVIRKelnlsELP-IIAMI 807
Cdd:cd17596      3 ILVVDD-EVRSLEALRRTLEEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRE-----RWPeVVRII 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1237881481  808 ------ANTMLADKNKAldcGMNDYIEKPFNINKLFSIMR 841
Cdd:cd17596     77 isgytdSEDIIAGINEA---GIYQYLTKPWHPDQLLLTVR 113
 
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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